You are on page 1of 15

Prolactin

Prolactin (PRL), also known as luteotropic


PRL
hormone or luteotropin, is a protein best known
for its role in enabling Mammals (and Birds), Available structures
usually females, to produce milk. It is influential PDB Ortholog search: PDBe (https://www.ebi.ac.uk/pdbe/sear
in over 300 separate processes in various chResults.html?display=both&term=P06879%20or%20P
vertebrates, including humans.[5] Prolactin is 01236) RCSB (http://www.rcsb.org/pdb/search/smartSub
secreted from the pituitary gland in response to query.do?smartSearchSubtype=UpAccessionIdQuery&ac
eating, mating, estrogen treatment, ovulation and cessionIdList=P06879,P01236)
nursing. It is secreted heavily in pulses in between
List of PDB id codes
these events. Prolactin plays an essential role in
metabolism, regulation of the immune system and 1RW5 (https://www.rcsb.org/structure/1RW5), 2Q98 (https://
pancreatic development. www.rcsb.org/structure/2Q98), 3D48 (https://www.rcsb.org/s
tructure/3D48), 3EW3 (https://www.rcsb.org/structure/3EW
Discovered in non-human animals around 1930
3), 3MZG (https://www.rcsb.org/structure/3MZG), 3N06 (http
by Oscar Riddle[6] and confirmed in humans in
s://www.rcsb.org/structure/3N06), 3N0P (https://www.rcsb.or
1970 by Henry Friesen,[7] prolactin is a peptide
g/structure/3N0P), 3NCB (https://www.rcsb.org/structure/3N
hormone, encoded by the PRL gene.[8]
CB), 3NCC (https://www.rcsb.org/structure/3NCC), 3NCE (h
In mammals, prolactin is associated with milk ttps://www.rcsb.org/structure/3NCE), 3NCF (https://www.rcs
production; in fish it is thought to be related to the b.org/structure/3NCF), 3NPZ (https://www.rcsb.org/structur
control of water and salt balance. Prolactin also e/3NPZ)
acts in a cytokine-like manner and as an important
regulator of the immune system. It has important Identifiers
cell cycle-related functions as a growth-, Aliases PRL (https://www.genenames.org/cgi-bin/gene_symbol
differentiating- and anti-apoptotic factor. As a _report?hgnc_id=9445), GHA1, prolactin
growth factor, binding to cytokine-like receptors,
External OMIM: 176760 (https://omim.org/entry/176760) MGI:
it influences hematopoiesis and angiogenesis, and
IDs 97762 (http://www.informatics.jax.org/marker/MGI:977
is involved in the regulation of blood clotting
62) HomoloGene: 732 (https://www.ncbi.nlm.nih.gov/e
through several pathways. The hormone acts in
ntrez/query.fcgi?cmd=Retrieve&db=homologene&dopt
endocrine, autocrine and paracrine manner
=HomoloGene&list_uids=732) GeneCards: PRL (http
through the prolactin receptor and numerous
s://www.genecards.org/cgi-bin/carddisp.pl?gene=PRL)
cytokine receptors.[5]
Gene location (Human)
Pituitary prolactin secretion is regulated by
endocrine neurons in the hypothalamus. The most
important of these are the neurosecretory
tuberoinfundibulum (TIDA) neurons of the
arcuate nucleus that secrete dopamine (aka
Prolactin Inhibitory Hormone) to act on the D2
receptors of lactotrophs, causing inhibition of Chr. Chromosome 6 (human)[1]
prolactin secretion. Thyrotropin-releasing factor
(thyrotropin-releasing hormone) has a stimulatory
effect on prolactin release, however prolactin is
the only adenohypophyseal hormone whose
Band 6p22.3 Start 22,287,244 bp[1]
principal control is inhibitory.
Several variants and forms are known per species. End 22,302,826 bp[1]
Many fish have variants prolactin A and prolactin
Gene location (Mouse)
B. Most vertebrates including humans also have
the closely related somatolactin. In humans, three
smaller (4, 16 and 22 kDa) and several larger (so
called big and big-big) variants exist.

Contents Chr. Chromosome 13 (mouse)[2]

Functions
Functions in other vertebrate
species
Regulation Band 13 A3.1|13 12.25 cM Start 27,057,570 bp[2]

Structure and isoforms End 27,065,205 bp[2]


Prolactin receptor Gene ontology
Diagnostic use
Molecular • prolactin receptor binding (http://amigo.geneontolo
Units and unit conversions function gy.org/amigo/term/GO:0005148)
Reference ranges • protein binding (http://amigo.geneontology.org/ami
Inter-method variability
go/term/GO:0005515)
Conditions • hormone activity (http://amigo.geneontology.org/a
Elevated levels
migo/term/GO:0005179)
Decreased levels
In medicine
Cellular • extracellular region (http://amigo.geneontology.or
component g/amigo/term/GO:0005576)
See also
• endosome lumen (http://amigo.geneontology.org/a
References
migo/term/GO:0031904)
External links
• secretory granule (http://amigo.geneontology.org/a
migo/term/GO:0030141)
• extracellular space (http://amigo.geneontology.or
Functions g/amigo/term/GO:0005615)
Prolactin has a wide variety of effects. It Biological • female pregnancy (http://amigo.geneontology.org/
stimulates the mammary glands to produce milk process amigo/term/GO:0007565)
(lactation): increased serum concentrations of • cellular protein metabolic process (http://amigo.ge
prolactin during pregnancy cause enlargement of neontology.org/amigo/term/GO:0044267)
the mammary glands and prepare for milk
• cell surface receptor signaling pathway (http://ami
production, which normally starts when levels of
go.geneontology.org/amigo/term/GO:0007166)
progesterone fall by the end of pregnancy and a
• JAK-STAT cascade involved in growth hormone
suckling stimulus is present. Prolactin plays an
signaling pathway (http://amigo.geneontology.org/a
important role in maternal behavior.[9]
migo/term/GO:0060397)
In general, dopamine inhibits prolactin[10] but this • lactation (http://amigo.geneontology.org/amigo/ter
process has feedback mechanisms.[11] m/GO:0007595)
• cell proliferation (http://amigo.geneontology.org/a
Elevated levels of prolactin decrease the levels of migo/term/GO:0008283)
sex hormones — estrogen in women and • positive regulation of JAK-STAT cascade (http://a
testosterone in men.[12] The effects of mildly migo.geneontology.org/amigo/term/GO:0046427)
elevated levels of prolactin are much more • regulation of multicellular organism growth (http://
variable, in women, substantially increasing or amigo.geneontology.org/amigo/term/GO:0040014)
decreasing estrogen levels.
Prolactin is sometimes classified as a • regulation of receptor activity (http://amigo.geneon
gonadotropin[13] although in humans it has only a tology.org/amigo/term/GO:0010469)
weak luteotropic effect while the effect of • negative regulation of endothelial cell proliferation
suppressing classical gonadotropic hormones is (http://amigo.geneontology.org/amigo/term/GO:000
more important.[14] Prolactin within the normal 1937)
reference ranges can act as a weak gonadotropin, • negative regulation of angiogenesis (http://amigo.
but at the same time suppresses GnRH secretion. geneontology.org/amigo/term/GO:0016525)
The exact mechanism by which it inhibits GnRH • positive regulation of pri-miRNA transcription from
is poorly understood. Although expression of RNA polymerase II promoter (http://amigo.geneonto
prolactin receptors (PRL-R) have been logy.org/amigo/term/GO:1902895)
demonstrated in rat hypothalamus, the same has • childbirth
not been observed in GnRH neurons.[15] • response to nutrient (http://amigo.geneontology.or
Physiologic levels of prolactin in males enhance g/amigo/term/GO:0007584)
luteinizing hormone-receptors in Leydig cells,
• circadian rhythm (http://amigo.geneontology.org/a
resulting in testosterone secretion, which leads to
migo/term/GO:0007623)
spermatogenesis.[16]
• positive regulation of cell proliferation (http://amig
Prolactin also stimulates proliferation of o.geneontology.org/amigo/term/GO:0008284)
oligodendrocyte precursor cells. These cells • response to organic cyclic compound (http://amig
differentiate into oligodendrocytes, the cells o.geneontology.org/amigo/term/GO:0014070)
responsible for the formation of myelin coatings • regulation of ossification (http://amigo.geneontolog
on axons in the central nervous system.[17] y.org/amigo/term/GO:0030278)
• response to estradiol (http://amigo.geneontology.o
Other actions include contributing to pulmonary rg/amigo/term/GO:0032355)
surfactant synthesis of the fetal lungs at the end of • response to lipopolysaccharide (http://amigo.gene
the pregnancy and immune tolerance of the fetus ontology.org/amigo/term/GO:0032496)
by the maternal organism during pregnancy.
• cellular response to hormone stimulus (http://amig
Prolactin promotes neurogenesis in maternal and
o.geneontology.org/amigo/term/GO:0032870)
fetal brains.[18][19]
• multicellular organismal response to stress (http://
amigo.geneontology.org/amigo/term/GO:0033555)
Functions in other vertebrate • response to drug (http://amigo.geneontology.org/a
migo/term/GO:0042493)
species
• ovulation cycle (http://amigo.geneontology.org/ami
The primary function of prolactin in fish is
go/term/GO:0042698)
osmoregulation,[20] i.e., controlling the movement
• response to ethanol (http://amigo.geneontology.or
of water and salts between the tissues of the fish
g/amigo/term/GO:0045471)
and the surrounding water. Like mammals,
• positive regulation of epithelial cell proliferation (ht
however, prolactin in fish also has reproductive
tp://amigo.geneontology.org/amigo/term/GO:005067
functions, including promoting sexual maturation
9)
and inducing breeding cycles, as well as brooding
• mammary gland development (http://amigo.geneo
and parental care.[21] In the South American
ntology.org/amigo/term/GO:0030879)
discus, prolactin may also regulate the production
• response to nutrient levels (http://amigo.geneontol
of a skin secretion that provides food for larval
ogy.org/amigo/term/GO:0031667)
fry.[22] An increase in brooding behaviour caused
• positive regulation of lactation (http://amigo.geneo
by prolactin has been reported in hens.[23]
ntology.org/amigo/term/GO:1903489)
Prolactin and its receptor are expressed in the Sources:Amigo (http://amigo.geneontology.org/) / QuickGO (http
skin, specifically in the hair follicles, where they s://www.ebi.ac.uk/QuickGO/)
regulate hair growth and moulting in an autocrine
Orthologs
fashion.[24][25] Elevated levels of prolactin can
inhibit hair growth,[26] and knock-out mutations Species Human Mouse
in the prolactin gene cause increased hair length Entrez
in cattle[27] and mice.[25] Conversely, mutations 5617 (https://www.ncbi.nlm. 19109 (https://www.ncbi.nl
in the prolactin receptor can cause reduced hair nih.gov/entrez/query.fcgi?d m.nih.gov/entrez/query.fcg
growth, resulting in the "slick" phenotype in b=gene&cmd=retrieve&dop i?db=gene&cmd=retrieve&
cattle.[27][28] Additionally, prolactin delays hair t=default&list_uids=5617&r dopt=default&list_uids=191
regrowth in mice.[29] n=1) 09&rn=1)

Analogous to its effects on hair growth and Ensembl


shedding in mammals, prolactin in birds controls ENSG00000172179 (http:// ENSMUSG00000021342
the moulting of feathers,[30] as well as the age at www.ensembl.org/Homo_s (http://www.ensembl.org/M
onset of feathering in both turkeys and apiens/geneview?gene=EN us_musculus/geneview?ge
chickens.[31] SG00000172179;db=core) ne=ENSMUSG000000213
42;db=core)

Regulation UniProt
P01236 (https://www.unipro P06879 (https://www.unipro
In humans, prolactin is produced at least in the
t.org/uniprot/P01236) t.org/uniprot/P06879)
anterior pituitary, decidua, myometrium, breast,
lymphocytes, leukocytes and prostate.[32][33]
RefSeq
NM_000948 (https://www.n NM_001163530 (https://ww
Pituitary PRL is controlled by the Pit-1 (mRNA)
cbi.nlm.nih.gov/entrez/view w.ncbi.nlm.nih.gov/entrez/vi
transcription factor that binds to the prolactin
er.fcgi?val=NM_000948) ewer.fcgi?val=NM_001163
gene at several sites. Ultimately dopamine,
NM_001163558 (https://ww 530)
extrapituitary PRL is controlled by a superdistal
w.ncbi.nlm.nih.gov/entrez/vi NM_011164 (https://www.n
promoter and apparently unaffected by
ewer.fcgi?val=NM_001163 cbi.nlm.nih.gov/entrez/view
dopamine.[33] The thyrotropin-releasing hormone
558) er.fcgi?val=NM_011164)
and the vasoactive intestinal peptide stimulate the
secretion of prolactin in experimental settings,
RefSeq
however their physiological influence is unclear. NP_000939 (https://www.n NP_001157002 (https://ww
(protein)
The main stimulus for prolactin secretion is cbi.nlm.nih.gov/entrez/view w.ncbi.nlm.nih.gov/entrez/vi
suckling, the effect of which is neuronally er.fcgi?val=NP_000939) ewer.fcgi?val=NP_0011570
mediated.[34] A key regulator of prolactin NP_001157030 (https://ww 02)
production is estrogens that enhance growth of w.ncbi.nlm.nih.gov/entrez/vi NP_035294 (https://www.n
prolactin-producing cells and stimulate prolactin ewer.fcgi?val=NP_0011570 cbi.nlm.nih.gov/entrez/view
production directly, as well as suppressing 30) er.fcgi?val=NP_035294)
dopamine.
Location Chr 6: 22.29 – 22.3 Mb (ht Chr 13: 27.06 – 27.07 Mb
In decidual cells and in lymphocytes the distal
(UCSC) tps://genome.ucsc.edu/cgi (https://genome.ucsc.edu/
promoter and thus prolactin expression is
-bin/hgTracks?org=Human cgi-bin/hgTracks?org=Mou
stimulated by cAMP. Responsivness to cAMP is
&db=hg38&position=chr6: se&db=mm0&position=chr
mediated by an imperfect cAMP–responsive
22287244-22302826) 13:27057570-27065205)
element and two CAAT/enhancer binding proteins
PubMed [3] [4]
(C/EBP).[33] Progesterone upregulates prolactin
search
synthesis in the endometrium and decreases it in
myometrium and breast glandular tissue.[35] Wikidata

Breast and other tissues may express the Pit-1 View/Edit Human View/Edit Mouse
promoter in addition to the distal promoter.
Extrapituitary production of prolactin is thought to be special to humans and primates and may serve mostly tissue-specific paracrine
and autocrine purposes. It has been hypothesized that in vertebrates such as mice a similar tissue-specific effect is achieved by a large
family of prolactin-like proteins controlled by at least 26 paralogous PRL genes not present in primates.[33]

Vasoactive intestinal peptide and peptide histidine isoleucine help to regulate prolactin secretion in humans, but the functions of these
hormones in birds can be quite different.[36]

Prolactin follows diurnal and ovulatory cycles. Prolactin levels peak during REM sleep and in the early morning. Many mammals
experience a seasonal cycle.

During pregnancy, high circulating concentrations of estrogen and progesterone increase prolactin levels by 10- to 20-fold. Estrogen
and progesterone inhibit the stimulatory effects of prolactin on milk production. The abrupt drop of estrogen and progesterone levels
following delivery allow prolactin—which temporarily remains high—to induce lactation.

Sucking on the nipple offsets the fall in prolactin as the internal stimulus for them is removed. The sucking activates
mechanoreceptors in and around the nipple. These signals are carried by nerve fibers through the spinal cord to the hypothalamus,
where changes in the electrical activity of neurons that regulate the pituitary gland increase prolactin secretion. The suckling stimulus
also triggers the release of oxytocin from the posterior pituitary gland, which triggers milk let-down: Prolactin controls milk
production (lactogenesis) but not the milk-ejection reflex; the rise in prolactin fills the breast with milk in preparation for the next
feed.

In usual circumstances, in the absence of galactorrhea, lactation ceases within one or two weeks following the end of breastfeeding.

Levels can rise after exercise, high-protein meals, minor surgical procedures,[37] following epileptic seizures[38] or due to physical or
emotional stress.[39][40] In a study on female volunteers under hypnosis, prolactin surges resulted from the evocation, with rage, of
humiliating experiences, but not from the fantasy of nursing.[40]

Hypersecretion is more common than hyposecretion. Hyperprolactinemia is the most frequent abnormality of the anterior pituitary
tumors, termed prolactinomas. Prolactinomas may disrupt the hypothalamic-pituitary-gonadal axis as prolactin tends to suppress the
secretion of GnRH from the hypothalamus and in turn decreases the secretion of follicle-stimulating hormone (FSH) and luteinizing
hormone (LH) from the anterior pituitary, therefore disrupting the ovulatory cycle.[41] Such hormonal changes may manifest as
amenorrhea and infertility in females as well as impotence in males. Inappropriate lactation (galactorrhoea) is another important
clinical sign of prolactinomas.

Structure and isoforms


The structure of prolactin is similar to that of growth hormone and placental lactogen. The molecule is folded due to the activity of
three disulfide bonds. Significant heterogeneity of the molecule has been described, thus bioassays and immunoassays can give
different results due to differing glycosylation, phosphorylation and sulfation, as well as degradation. The non-glycosylated form of
prolactin is the dominant form that is secreted by the pituitary gland.

The three different sizes of prolactin are:

Little prolactin—the predominant form.[42] It has a molecular weight of appxoximately 22-kDa.[42] It is a single-chain
polypeptide of 198 amino acids and is apparently the result of removal of some amino acids.
Big prolactin—approximately 48 kDa.[42] It may be the product of interaction of several prolactin molecules. It
appears to have little, if any, biological activity.[43]
Big big prolactin—approximately 150 kDa.[42] It appears to have a low biological activity.[44]
The levels of larger ones are somewhat higher during the early postpartum period.[45]

Prolactin receptor
Prolactin receptors are present in the mammillary glands, ovaries, pituitary glands, heart, lung, thymus, spleen, liver, pancreas, kidney,
adrenal gland, uterus, skeletal muscle, skin and areas of the central nervous system.[46] When prolactin binds to the receptor, it causes
it to dimerize with another prolactin receptor. This results in the activation of Janus kinase 2, a tyrosine kinase that initiates the JAK-
STAT pathway. Activation also results in the activation of mitogen-activated protein kinases and Src kinase.[46]

Human prolactin receptors are insensitive to mouse prolactin.[47]

Diagnostic use
Prolactin levels may be checked as part of a sex hormone workup, as elevated prolactin secretion can suppress the secretion of FSH
and GnRH, leading to hypogonadism and sometimes causing erectile dysfunction.

Prolactin levels may be of some use in distinguishing epileptic seizures from psychogenic non-epileptic seizures. The serum prolactin
level usually rises following an epileptic seizure.[48]

Units and unit conversions


The serum concentration of prolactin can be given in mass concentration (µg/L or ng/mL), molar concentration (nmol/L or pmol/L) or
in international units (typically mIU/L). The current IU is calibrated against the third International Standard for Prolactin, IS
84/500.[49][50] Reference ampoules of IS 84/500 contain 2.5 µg of lyophilized human prolactin[51] and have been assigned an activity
of .053 International Units.[49][50] Measurements that are calibrated against the current international standard can be converted into
mass units using this ratio of grams to IUs;[52] prolactin concentrations expressed in mIU/L can be converted to µg/L by dividing by
21.2. Previous standards use other ratios.[53][54][55][56]

The first International Reference Preparation (or IRP) of human Prolactin for Immunoassay was established in 1978 (75/504 1st IRP
for human Prolactin) at a time when purified human prolactin was in short supply.[52][53] Previous standards relied on prolactin from
animal sources.[56] Purified human prolactin was scarce, heterogeneous, unstable and difficult to characterize. A preparation labelled
81/541 was distributed by the WHO Expert Committee on Biological Standardization without official status and given the assigned
value of 50 mIU/ampoule based on an earlier collaborative study.[52][54] It was determined that this preparation behaved anomalously
in certain immunoassays and was not suitable as an IS.[52]

Three different human pituitary extracts containing prolactin were subsequently obtained as candidates for an IS. These were
distributed into ampoules coded 83/562, 83/573 and 84/500.[49][50][52][55] Collaborative studies involving 20 different laboratories
found little difference between these three preparations. 83/562 appeared to be the most stable. This preparation was largely free of
dimers and polymers of prolactin. On the basis of these investigations 83/562 was established as the Second IS for human
Prolactin.[55] Once stocks of these ampoules were depleted, 84/500 was established as the Third IS for human Prolactin.[49][52]

Reference ranges
General guidelines for diagnosing prolactin excess (hyperprolactinemia) define the upper threshold of normal prolactin at 25 µg/L for
women and 20 µg/L for men.[46] Similarly, guidelines for diagnosing prolactin deficiency (hypoprolactinemia) are defined as
prolactin levels below 3 µg/L in women[57][58] and 5 µg/L in men.[59][60][61] However, different assays and methods for measuring
prolactin are employed by different laboratories and as such the serum reference range for prolactin is often determined by the
laboratory performing the measurement.[46][62] Furthermore, prolactin levels also vary factors including age,[63] sex,[63] menstrual
cycle stage[63] and pregnancy.[63] The circumstances surrounding a given prolactin measurement (assay, patient condition, etc.) must
therefore be considered before the measurement can be accurately interpreted.[46]

The following chart illustrates the variations seen in normal prolactin measurements across different populations. Prolactin values
were obtained from specific control groups of varying sizes using the IMMULITE assay.[63]

Typical prolactin values


Proband Prolactin, µg/L
women, follicular
12.1
phase (n = 803)
women, luteal
13.9
phase (n = 699)
women, mid-
17
cycle (n = 53)
women, whole
13.0
cycle (n = 1555)
women,
pregnant, 1st 16
trimester (n = 39)
women,
pregnant, 2nd 49
trimester (n = 52)
women,
pregnant, 3rd 113
trimester (n = 54)
Men, 21–30 (n =
9.2
50)
Men, 31–40 (n =
7.1
50)
Men, 41–50 (n = 7.0
50)
Men, 51–60 (n =
6.2
50)
Men, 61–70 (n =
6.9
50)

Inter-method variability
The following table illustrates variability in reference ranges of serum prolactin between some commonly used assay methods (as of
2008), using a control group of healthy health care professionals (53 males, age 20–64 years, median 28 years; 97 females, age 19–59
years, median 29 years) in Essex, England:[62]
Mean Lower limit Upper limit
Prolactin 2.5th percentile 97.5th percentile

Assay method µg/L mIU/L µg/L mIU/L µg/L mIU/L


Females
Centaur 7.92 168 3.35 71 16.4 348
Immulite 9.25 196 3.54 75 18.7 396
Access 9.06 192 3.63 77 19.3 408

AIA 9.52[64] 257[64] 3.89[64] 105[64] 20.3[64] 548[64]


Elecsys 10.5 222 4.15 88 23.2 492
Architect 10.6 225 4.62 98 21.1 447
Males
Access 6.89 146 2.74 58 13.1 277
Centaur 7.88 167 2.97 63 12.4 262
Immulite 7.45 158 3.30 70 13.3 281

AIA 7.81[64] 211[64] 3.30[64] 89[64] 13.5[64] 365[64]


Elecsys 8.49 180 3.40 72 15.6 331
Architect 8.87 188 4.01 85 14.6 310

An example usage of table above is, if using the Centaur assay to estimate prolactin values in µg/L for females, the mean is 7.92 µg/L
and the reference range is 3.35–16.4 µg/L.

Conditions

Elevated levels
Hyperprolactinaemia, or excess serum prolactin, is associated with hypoestrogenism, anovulatory infertility, oligomenorrhoea,
amenorrhoea, unexpected lactation and loss of libido in women and erectile dysfunction and loss of libido in men.[65]

Physiological Pharmacological Pathological

Coitus Anesthetics Hypothalamic-pituitary


stalk damage Pituitary
Exercise Anticonvulsant
Lactation Antihistamines Granulomas Acromegaly
Pregnancy (H2) Idiopathic
Infiltrations
Sleep Antihypertensives Lymphocytic
Radiation
Stress Cholinergic hypophysitis or
Rathke's cyst parasellar mass
agonist
Depression Trauma
Drug-induced Macroadenoma
hypersecretion Pituitary stalk (compressive)
Catecholamine resection Macroprolactinemia
depletor Suprasellar surgery Plurihumoral
Dopamine adenoma
Tumors
receptor blockers Prolactinoma
Dopamine Craniopharyngioma Systemic disorders
synthesis inhibitor Germinoma
Estrogens
Oral Hypothalamic Chest-neurologic
contraceptives metastases chest wall trauma
Oral Meningioma Herpes Zoster
contraceptive Suprasellar Chronic renal
withdrawal pituitary mass failure
Neuroleptics extension Cirrhosis
Antipsychotics Surgery Cranial radiation
Neuropeptides Epileptic seizures
Opiates and opiate Polycystic ovarian
antagonists disease
Pseudocyesis
Chronic low levels
of thyroid hormone

Decreased levels
Hypoprolactinemia, or serum prolactin deficiency, is associated with ovarian dysfunction in women,[57][58] and arteriogenic erectile
dysfunction, premature ejaculation,[59] oligozoospermia, asthenospermia, hypofunction of seminal vesicles and hypoandrogenism[60]
in men. In one study, normal sperm characteristics were restored when prolactin levels were raised to normal values in
hypoprolactinemic men.[61]

Hypoprolactinemia can result from hypopituitarism, excessive dopaminergic action in the tuberoinfundibular pathway and ingestion
of D2 receptor agonists such as bromocriptine.

While there is evidence that women who smoke tend to breast feed for shorter periods, there is a wide variation of breast-feeding rates
in women who do smoke. This suggest that psychosocial factors rather than physiological mechanisms (e.g., nicotine suppressing
prolactin levels) are responsible for the lower rates of breast feeding in women who do smoke.[66][67]

In medicine
Prolactin is available commercially for use in animals, but not in humans.[68] It is used to stimulate lactation in animals.[68] The
biological half-life of prolactin in humans is around 15–20 minutes.[69] The D2 receptor is involved in the regulation of prolactin
secretion, and agonists of the receptor such as bromocriptine and cabergoline decrease prolactin levels while antagonists of the
receptor such as domperidone, metoclopramide, haloperidol, risperidone, and sulpiride increase prolactin levels.[70] D2 receptor
antagonists like domperidone, metoclopramide, and sulpiride are used as galactogogues to increase prolactin secretion in pituitary
gland and induce lactation in humans.[71]

See also
Breast-feeding
Epileptic seizure
Hyperprolactinaemia
Hypothalamic–pituitary–prolactin axis
Male lactation
Prolactin modulator
Prolactin receptor
Prolactin-releasing hormone
Prolactinoma
Weaning
References
1. GRCh38: Ensembl release 89: ENSG00000172179 (http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Sum
mary?db=core;g=ENSG00000172179) - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021342 (http://May2017.archive.ensembl.org/Mus_musculus/Gene/
Summary?db=core;g=ENSMUSG00000021342) - Ensembl, May 2017
3. "Human PubMed Reference:" (https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pub
med&from_uid=5617). National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:" (https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pub
med&from_uid=19109). National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Bole-Feysot C, Goffin V, Edery M, Binart N, Kelly PA (June 1998). "Prolactin (PRL) and its receptor: actions, signal
transduction pathways and phenotypes observed in PRL receptor knockout mice". Endocrine Reviews. 19 (3): 225–
68. doi:10.1210/er.19.3.225 (https://doi.org/10.1210%2Fer.19.3.225). PMID 9626554 (https://www.ncbi.nlm.nih.gov/p
ubmed/9626554).
6. Bates R, Riddle O (November 1935). "The preparation of prolactin" (http://jpet.aspetjournals.org/content/55/3/365.abs
tract). Journal of Pharmacology and Experimental Therapeutics. 55 (3): 365–371.
7. Friesen H, Guyda H, Hardy J (December 1970). "The biosynthesis of human growth hormone and prolactin" (http://jc
em.endojournals.org/content/31/6/611.abstract). The Journal of Clinical Endocrinology and Metabolism. 31 (6): 611–
24. doi:10.1210/jcem-31-6-611 (https://doi.org/10.1210%2Fjcem-31-6-611). PMID 5483096 (https://www.ncbi.nlm.nih.
gov/pubmed/5483096).
8. Evans AM, Petersen JW, Sekhon GS, DeMars R (May 1989). "Mapping of prolactin and tumor necrosis factor-beta
genes on human chromosome 6p using lymphoblastoid cell deletion mutants". Somatic Cell and Molecular Genetics.
15 (3): 203–13. doi:10.1007/BF01534871 (https://doi.org/10.1007%2FBF01534871). PMID 2567059 (https://www.ncb
i.nlm.nih.gov/pubmed/2567059).
9. Lucas BK, Ormandy CJ, Binart N, Bridges RS, Kelly PA (October 1998). "Null mutation of the prolactin receptor gene
produces a defect in maternal behavior". Endocrinology. 139 (10): 4102–7. doi:10.1210/endo.139.10.6243 (https://do
i.org/10.1210%2Fendo.139.10.6243). PMID 9751488 (https://www.ncbi.nlm.nih.gov/pubmed/9751488).
10. Ben-Jonathan N (1985). "Dopamine: a prolactin-inhibiting hormone". Endocrine Reviews. 6 (4): 564–89.
doi:10.1210/edrv-6-4-564 (https://doi.org/10.1210%2Fedrv-6-4-564). PMID 2866952 (https://www.ncbi.nlm.nih.gov/pu
bmed/2866952).
11. Freeman ME, Kanyicska B, Lerant A, Nagy G (October 2000). "Prolactin: structure, function, and regulation of
secretion". Physiological Reviews. 80 (4): 1523–631. doi:10.1152/physrev.2000.80.4.1523 (https://doi.org/10.1152%2
Fphysrev.2000.80.4.1523). PMID 11015620 (https://www.ncbi.nlm.nih.gov/pubmed/11015620).
12. Prolactinoma (http://www.mayoclinic.com/health/prolactinoma/DS00532)—Mayo Clinic
13. Hoehn K, Marieb EN (2007). Human Anatomy & Physiology. San Francisco: Pearson Benjamin Cummings. p. 605.
ISBN 978-0-8053-5909-1.
14. Gonadotropins (https://meshb.nlm.nih.gov/record/ui?name=Gonadotropins) at the US National Library of Medicine
Medical Subject Headings (MeSH)
15. Grattan DR, Jasoni CL, Liu X, Anderson GM, Herbison AE (September 2007). "Prolactin regulation of gonadotropin-
releasing hormone neurons to suppress luteinizing hormone secretion in mice". Endocrinology. 148 (9): 4344–51.
doi:10.1210/en.2007-0403 (https://doi.org/10.1210%2Fen.2007-0403). PMID 17569755 (https://www.ncbi.nlm.nih.go
v/pubmed/17569755).
16. Hair WM, Gubbay O, Jabbour HN, Lincoln GA (July 2002). "Prolactin receptor expression in human testis and
accessory tissues: localization and function". Molecular Human Reproduction. 8 (7): 606–11.
doi:10.1093/molehr/8.7.606 (https://doi.org/10.1093%2Fmolehr%2F8.7.606). PMID 12087074 (https://www.ncbi.nlm.
nih.gov/pubmed/12087074).
17. Gregg C, Shikar V, Larsen P, Mak G, Chojnacki A, Yong VW, Weiss S (February 2007). "White matter plasticity and
enhanced remyelination in the maternal CNS". The Journal of Neuroscience. 27 (8): 1812–23.
doi:10.1523/JNEUROSCI.4441-06.2007 (https://doi.org/10.1523%2FJNEUROSCI.4441-06.2007). PMID 17314279 (h
ttps://www.ncbi.nlm.nih.gov/pubmed/17314279).
18. Shingo T, Gregg C, Enwere E, Fujikawa H, Hassam R, Geary C, Cross JC, Weiss S (January 2003). "Pregnancy-
stimulated neurogenesis in the adult female forebrain mediated by prolactin". Science. 299 (5603): 117–20.
doi:10.1126/science.1076647 (https://doi.org/10.1126%2Fscience.1076647). PMID 12511652 (https://www.ncbi.nlm.
nih.gov/pubmed/12511652).
19. Larsen CM, Grattan DR (February 2012). "Prolactin, neurogenesis, and maternal behaviors". Brain, Behavior, and
Immunity. 26 (2): 201–9. doi:10.1016/j.bbi.2011.07.233 (https://doi.org/10.1016%2Fj.bbi.2011.07.233).
PMID 21820505 (https://www.ncbi.nlm.nih.gov/pubmed/21820505).
20. Sakamoto T, McCormick SD (May 2006). "Prolactin and growth hormone in fish osmoregulation". General and
Comparative Endocrinology. 147 (1): 24–30. doi:10.1016/j.ygcen.2005.10.008 (https://doi.org/10.1016%2Fj.ygcen.20
05.10.008). PMID 16406056 (https://www.ncbi.nlm.nih.gov/pubmed/16406056).
21. Whittington CM, Wilson AB (September 2013). "The role of prolactin in fish reproduction" (https://ses.library.usyd.ed
u.au/bitstream/2123/9291/2/GCE_PRL_in_fish_reproduction_postprint.pdf) (PDF). General and Comparative
Endocrinology. 191: 123–36. doi:10.1016/j.ygcen.2013.05.027 (https://doi.org/10.1016%2Fj.ygcen.2013.05.027).
PMID 23791758 (https://www.ncbi.nlm.nih.gov/pubmed/23791758).
22. Khong HK, Kuah MK, Jaya-Ram A, Shu-Chien AC (May 2009). "Prolactin receptor mRNA is upregulated in discus
fish (Symphysodon aequifasciata) skin during parental phase". Comparative Biochemistry and Physiology Part B:
Biochemistry and Molecular Biology. 153 (1): 18–28. doi:10.1016/j.cbpb.2009.01.005 (https://doi.org/10.1016%2Fj.cb
pb.2009.01.005). PMID 19272315 (https://www.ncbi.nlm.nih.gov/pubmed/19272315).
23. Jiang RS, Xu GY, Zhang XQ, Yang N (June 2005). "Association of polymorphisms for prolactin and prolactin receptor
genes with broody traits in chickens". Poultry Science. 84 (6): 839–845. doi:10.1093/ps/84.6.839 (https://doi.org/10.1
093%2Fps%2F84.6.839). PMID 15971519 (https://www.ncbi.nlm.nih.gov/pubmed/15971519).
24. Foitzik K, Krause K, Nixon AJ, Ford CA, Ohnemus U, Pearson AJ, Paus R (May 2003). "Prolactin and Its Receptor
Are Expressed in Murine Hair Follicle Epithelium, Show Hair Cycle-Dependent Expression, and Induce Catagen" (htt
ps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1851183). The American Journal of Pathology. 162 (5): 1611–21.
doi:10.1016/S0002-9440(10)64295-2 (https://doi.org/10.1016%2FS0002-9440%2810%2964295-2). PMC 1851183 (h
ttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1851183). PMID 12707045 (https://www.ncbi.nlm.nih.gov/pubmed/1270
7045).
25. Craven AJ, Ormandy CJ, Robertson FG, Wilkins RJ, Kelly PA, Nixon AJ, Pearson AJ (June 2001). "Prolactin
Signaling Influences the Timing Mechanism of the Hair Follicle: Analysis of Hair Growth Cycles in Prolactin Receptor
Knockout Mice". Endocrinology. 142 (6): 2533–9. doi:10.1210/endo.142.6.8179 (https://doi.org/10.1210%2Fendo.14
2.6.8179). PMID 11356702 (https://www.ncbi.nlm.nih.gov/pubmed/11356702).
26. Foitzik K, Krause K, Conrad F, Nakamura M, Funk W, Paus R (March 2006). "Human scalp hair follicles are both a
target and a source of prolactin, which serves as an autocrine and/or paracrine promoter of apoptosis-driven hair
follicle regression" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1606541). The American Journal of Pathology.
168 (3): 748–56. doi:10.2353/ajpath.2006.050468 (https://doi.org/10.2353%2Fajpath.2006.050468). PMC 1606541 (h
ttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1606541). PMID 16507890 (https://www.ncbi.nlm.nih.gov/pubmed/1650
7890).
27. Littlejohn MD, Henty KM, Tiplady K, Johnson T, Harland C, Lopdell T, Sherlock RG, Li W, Lukefahr SD, Shanks BC,
Garrick DJ, Snell RG, Spelman RJ, Davis SR (December 2014). "Functionally reciprocal mutations of the prolactin
signalling pathway define hairy and slick cattle" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4284646). Nature
Communications. 5: 5861. doi:10.1038/ncomms6861 (https://doi.org/10.1038%2Fncomms6861). PMC 4284646 (http
s://www.ncbi.nlm.nih.gov/pmc/articles/PMC4284646). PMID 25519203 (https://www.ncbi.nlm.nih.gov/pubmed/255192
03).
28. Porto-Neto LR, Bickhart DM, Landaeta-Hernandez AJ, Utsunomiya YT, Pagan M, Jimenez E, Hansen PJ, Dikmen S,
Schroeder SG, Kim ES, Sun J, Crespo E, Amati N, Cole JB, Null DJ, Garcia JF, Reverter A, Barendse W, Sonstegard
TS (February 2018). "Convergent Evolution of Slick Coat in Cattle through Truncation Mutations in the Prolactin
Receptor" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5829098). Frontiers in Genetics. 9: 57.
doi:10.3389/fgene.2018.00057 (https://doi.org/10.3389%2Ffgene.2018.00057). PMC 5829098 (https://www.ncbi.nlm.
nih.gov/pmc/articles/PMC5829098). PMID 29527221 (https://www.ncbi.nlm.nih.gov/pubmed/29527221).
29. Craven AJ, Nixon AJ, Ashby MG, Ormandy CJ, Blazek K, Wilkins RJ, Pearson AJ (November 2006). "Prolactin
delays hair regrowth in mice". The Journal of Endocrinology. 191 (2): 415–25. doi:10.1677/joe.1.06685 (https://doi.or
g/10.1677%2Fjoe.1.06685). PMID 17088411 (https://www.ncbi.nlm.nih.gov/pubmed/17088411).
30. Dawson A (July 2006). "Control of molt in birds: association with prolactin and gonadal regression in starlings".
General and Comparative Endocrinology. 147 (3): 314–22. doi:10.1016/j.ygcen.2006.02.001 (https://doi.org/10.101
6%2Fj.ygcen.2006.02.001). PMID 16530194 (https://www.ncbi.nlm.nih.gov/pubmed/16530194).
31. Derks MF, Herrero-Medrano JM, Crooijmans RP, Vereijken A, Long JA, Megens HJ, Groenen MA (February 2018).
"Early and late feathering in turkey and chicken: same gene but different mutations" (https://www.ncbi.nlm.nih.gov/pm
c/articles/PMC5863816). Genetics Selection Evolution. 50 (1): 7. doi:10.1186/s12711-018-0380-3 (https://doi.org/10.
1186%2Fs12711-018-0380-3). PMC 5863816 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5863816).
PMID 29566646 (https://www.ncbi.nlm.nih.gov/pubmed/29566646).
32. Ben-Jonathan N, Mershon JL, Allen DL, Steinmetz RW (December 1996). "Extrapituitary prolactin: distribution,
regulation, functions, and clinical aspects". Endocrine Reviews. 17 (6): 639–69. doi:10.1210/edrv-17-6-639 (https://do
i.org/10.1210%2Fedrv-17-6-639). PMID 8969972 (https://www.ncbi.nlm.nih.gov/pubmed/8969972).
33. Gerlo S, Davis JR, Mager DL, Kooijman R (October 2006). "Prolactin in man: a tale of two promoters" (https://www.nc
bi.nlm.nih.gov/pmc/articles/PMC1891148). BioEssays. 28 (10): 1051–5. doi:10.1002/bies.20468 (https://doi.org/10.10
02%2Fbies.20468). PMC 1891148 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891148). PMID 16998840 (http
s://www.ncbi.nlm.nih.gov/pubmed/16998840).
34. Norman AW, Henry HL, eds. (2014). "III. Structure, Synthesis, Secretion, and Target Cells of the Hypothalamic
Releasing Hormones: E. Hypothalamic Control of Prolactin Secretion" (https://books.google.si/books?id=_renonjXq6
8C&pg=PA66). Hormones. Academic Press. p. 66. ISBN 9780080919065.
35. Zinger M, McFarland M, Ben-Jonathan N (February 2003). "Prolactin expression and secretion by human breast
glandular and adipose tissue explants". The Journal of Clinical Endocrinology and Metabolism. 88 (2): 689–96.
doi:10.1210/jc.2002-021255 (https://doi.org/10.1210%2Fjc.2002-021255). PMID 12574200 (https://www.ncbi.nlm.nih.
gov/pubmed/12574200).
36. Kulick RS, Chaiseha Y, Kang SW, Rozenboim I, El Halawani ME (July 2005). "The relative importance of vasoactive
intestinal peptide and peptide histidine isoleucine as physiological regulators of prolactin in the domestic turkey".
General and Comparative Endocrinology. 142 (3): 267–73. doi:10.1016/j.ygcen.2004.12.024 (https://doi.org/10.101
6%2Fj.ygcen.2004.12.024). PMID 15935152 (https://www.ncbi.nlm.nih.gov/pubmed/15935152).
37. Melmed S, Jameson JL (2005). "333 Disorders of the Anterior Pituitary and Hypothalamus" (http://highered.mcgraw-h
ill.com/sites/0071402357/information_center_view0/). In Jameson JN, Kasper DL, Harrison TR, Braunwald E, Fauci
AS, Hauser SL, Longo DL (eds.). Harrison's principles of internal medicine (16th ed.). New York: McGraw-Hill
Medical Publishing Division. ISBN 978-0-07-140235-4.
38. Mellers JD (August 2005). "The approach to patients with "non-epileptic seizures" " (https://www.ncbi.nlm.nih.gov/pm
c/articles/PMC1743326). Postgraduate Medical Journal. 81 (958): 498–504. doi:10.1136/pgmj.2004.029785 (https://d
oi.org/10.1136%2Fpgmj.2004.029785). PMC 1743326 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1743326).
PMID 16085740 (https://www.ncbi.nlm.nih.gov/pubmed/16085740).
39. "Prolactin" (https://www.nlm.nih.gov/medlineplus/ency/article/003718.htm). MedLine plus. Retrieved 24 October
2014.
40. Sobrinho LG (2003). "Prolactin, psychological stress and environment in humans: adaptation and maladaptation".
Pituitary. 6 (1): 35–9. doi:10.1023/A:1026229810876 (https://doi.org/10.1023%2FA%3A1026229810876).
PMID 14674722 (https://www.ncbi.nlm.nih.gov/pubmed/14674722).
41. "Etiology, diagnosis, and treatment of secondary amenorrhea" (http://www.uptodate.com/contents/etiology-diagnosis-
and-treatment-of-secondary-amenorrhea?detectedLanguage=en&source=search_result&search=etiology+of+second
ary+amenorrhea&selectedTitle=1%7E30&provider=noProvider). Retrieved 7 November 2013.
42. Sabharwal P, Glaser R, Lafuse W, Varma S, Liu Q, Arkins S, Kooijman R, Kutz L, Kelley KW, Malarkey WB (August
1992). "Prolactin synthesized and secreted by human peripheral blood mononuclear cells: an autocrine growth factor
for lymphoproliferation" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC49781). Proceedings of the National
Academy of Sciences of the United States of America. 89 (16): 7713–6. doi:10.1073/pnas.89.16.7713 (https://doi.org/
10.1073%2Fpnas.89.16.7713). PMC 49781 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC49781). PMID 1502189
(https://www.ncbi.nlm.nih.gov/pubmed/1502189)., in turn citing: Kiefer KA, Malarkey WB (January 1978). "Size
heterogeneity of human prolactin in CSF and serum: experimental conditions that alter gel filtration patterns". The
Journal of Clinical Endocrinology and Metabolism. 46 (1): 119–24. doi:10.1210/jcem-46-1-119 (https://doi.org/10.121
0%2Fjcem-46-1-119). PMID 752015 (https://www.ncbi.nlm.nih.gov/pubmed/752015).
43. Garnier PE, Aubert ML, Kaplan SL, Grumbach MM (December 1978). "Heterogeneity of pituitary and plasma
prolactin in man: decreased affinity of "Big" prolactin in a radioreceptor assay and evidence for its secretion". The
Journal of Clinical Endocrinology and Metabolism. 47 (6): 1273–81. doi:10.1210/jcem-47-6-1273 (https://doi.org/10.1
210%2Fjcem-47-6-1273). PMID 263349 (https://www.ncbi.nlm.nih.gov/pubmed/263349).
44. Leite V, Cosby H, Sobrinho LG, Fresnoza MA, Santos MA, Friesen HG (October 1992). "Characterization of big, big
prolactin in patients with hyperprolactinaemia". Clinical Endocrinology. 37 (4): 365–72. doi:10.1111/j.1365-
2265.1992.tb02340.x (https://doi.org/10.1111%2Fj.1365-2265.1992.tb02340.x). PMID 1483294 (https://www.ncbi.nl
m.nih.gov/pubmed/1483294).
45. Kamel MA, Neulen J, Sayed GH, Salem HT, Breckwoldt M (September 1993). "Heterogeneity of human prolactin
levels in serum during the early postpartum period". Gynecological Endocrinology. 7 (3): 173–7.
doi:10.3109/09513599309152499 (https://doi.org/10.3109%2F09513599309152499). PMID 8291454 (https://www.nc
bi.nlm.nih.gov/pubmed/8291454).
46. Mancini T, Casanueva FF, Giustina A (March 2008). "Hyperprolactinemia and prolactinomas". Endocrinology and
Metabolism Clinics of North America. 37 (1): 67–99, viii. doi:10.1016/j.ecl.2007.10.013 (https://doi.org/10.1016%2Fj.e
cl.2007.10.013). PMID 18226731 (https://www.ncbi.nlm.nih.gov/pubmed/18226731).
47. Utama FE, LeBaron MJ, Neilson LM, Sultan AS, Parlow AF, Wagner KU, Rui H (March 2006). "Human prolactin
receptors are insensitive to mouse prolactin: implications for xenotransplant modeling of human breast cancer in
mice". The Journal of Endocrinology. 188 (3): 589–601. doi:10.1677/joe.1.06560 (https://doi.org/10.1677%2Fjoe.1.06
560). PMID 16522738 (https://www.ncbi.nlm.nih.gov/pubmed/16522738).
48. Banerjee S, Paul P, Talib VJ (August 2004). "Serum prolactin in seizure disorders". Indian Pediatrics. 41 (8): 827–31.
PMID 15347871 (https://www.ncbi.nlm.nih.gov/pubmed/15347871).
49. Schulster D, Gaines Das RE, Jeffcoate SL (April 1989). "International Standards for human prolactin: calibration by
international collaborative study". The Journal of Endocrinology. 121 (1): 157–66. doi:10.1677/joe.0.1210157 (https://
doi.org/10.1677%2Fjoe.0.1210157). PMID 2715755 (https://www.ncbi.nlm.nih.gov/pubmed/2715755).
50. "WHO Expert Committee on Biological Standardization" (http://whqlibdoc.who.int/trs/WHO_TRS_786.pdf) (PDF).
Thirty-ninth Report, WHO Technical Report Series. World Health Organization. 1989. Retrieved 3 June 2009.
"86.1520, WHO/BS documents: 86.1520 Add 1, 88.1596"
51. "WHO International Standard, Prolactin, Human. NIBSC code: 84/500, Instructions for use" (https://web.archive.org/w
eb/20111003214114/http://www.nibsc.ac.uk/documents/ifu/84-500.pdf) (PDF). NIBSC / Health Protection Agency.
1989. Archived from the original (http://www.nibsc.ac.uk/documents/ifu/84-500.pdf) (PDF) on 3 October 2011.
Retrieved 21 March 2011.
52. Canadian Society of Clinical Chemists (December 1992). "Canadian Society of Clinical Chemists position paper:
standardization of selected polypeptide hormone measurements". Clinical Biochemistry. 25 (6): 415–24.
doi:10.1016/0009-9120(92)90030-V (https://doi.org/10.1016%2F0009-9120%2892%2990030-V). PMID 1477965 (htt
ps://www.ncbi.nlm.nih.gov/pubmed/1477965).
53. Gaines Das RE, Cotes PM (January 1979). "International Reference Preparation of human prolactin for
immunoassay: definition of the International Unit, report of a collaborative study and comparison of estimates of
human prolactin made in various laboratories". The Journal of Endocrinology. 80 (1): 157–68.
doi:10.1677/joe.0.0800157 (https://doi.org/10.1677%2Fjoe.0.0800157). PMID 429949 (https://www.ncbi.nlm.nih.gov/p
ubmed/429949).
54. "WHO Expert Committee on Biological Standardization" (http://whqlibdoc.who.int/trs/WHO_TRS_725.pdf) (PDF).
Thirty-fifth Report, WHO Technical Report Series. World Health Organization. 1985. Retrieved 21 March 2011.
55. "WHO Expert Committee on Biological Standardization" (http://whqlibdoc.who.int/trs/WHO_TRS_760.pdf) (PDF).
Thirty-seventh Report, WHO Technical Report Series. World Health Organization. 1987. Retrieved 21 March 2011.
56. Bangham DR, Mussett MV, Stack-Dunne MP (1963). "THE SECOND INTERNATIONAL STANDARD FOR
PROLACTIN" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2555104). Bulletin of the World Health Organization.
29 (6): 721–8. PMC 2555104 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2555104). PMID 14107744 (https://ww
w.ncbi.nlm.nih.gov/pubmed/14107744).
57. Kauppila A, Martikainen H, Puistola U, Reinilä M, Rönnberg L (March 1988). "Hypoprolactinemia and ovarian
function". Fertility and Sterility. 49 (3): 437–41. doi:10.1016/s0015-0282(16)59769-6 (https://doi.org/10.1016%2Fs001
5-0282%2816%2959769-6). PMID 3342895 (https://www.ncbi.nlm.nih.gov/pubmed/3342895).
58. Schwärzler P, Untergasser G, Hermann M, Dirnhofer S, Abendstein B, Berger P (October 1997). "Prolactin gene
expression and prolactin protein in premenopausal and postmenopausal human ovaries". Fertility and Sterility. 68
(4): 696–701. doi:10.1016/S0015-0282(97)00320-8 (https://doi.org/10.1016%2FS0015-0282%2897%2900320-8).
PMID 9341613 (https://www.ncbi.nlm.nih.gov/pubmed/9341613).
59. Corona G, Mannucci E, Jannini EA, Lotti F, Ricca V, Monami M, Boddi V, Bandini E, Balercia G, Forti G, Maggi M
(May 2009). "Hypoprolactinemia: a new clinical syndrome in patients with sexual dysfunction". The Journal of Sexual
Medicine. 6 (5): 1457–66. doi:10.1111/j.1743-6109.2008.01206.x (https://doi.org/10.1111%2Fj.1743-6109.2008.0120
6.x). PMID 19210705 (https://www.ncbi.nlm.nih.gov/pubmed/19210705).
60. Gonzales GF, Velasquez G, Garcia-Hjarles M (1989). "Hypoprolactinemia as related to seminal quality and serum
testosterone". Archives of Andrology. 23 (3): 259–65. doi:10.3109/01485018908986849 (https://doi.org/10.3109%2F
01485018908986849). PMID 2619414 (https://www.ncbi.nlm.nih.gov/pubmed/2619414).
61. Ufearo CS, Orisakwe OE (September 1995). "Restoration of normal sperm characteristics in hypoprolactinemic
infertile men treated with metoclopramide and exogenous human prolactin". Clinical Pharmacology and
Therapeutics. 58 (3): 354–9. doi:10.1016/0009-9236(95)90253-8 (https://doi.org/10.1016%2F0009-9236%2895%299
0253-8). PMID 7554710 (https://www.ncbi.nlm.nih.gov/pubmed/7554710).
62. Table 2 (http://www.clinchem.org/cgi/content/full/54/10/1673/T2) in Beltran L, Fahie-Wilson MN, McKenna TJ,
Kavanagh L, Smith TP (October 2008). "Serum total prolactin and monomeric prolactin reference intervals
determined by precipitation with polyethylene glycol: evaluation and validation on common immunoassay platforms".
Clinical Chemistry. 54 (10): 1673–81. doi:10.1373/clinchem.2008.105312 (https://doi.org/10.1373%2Fclinchem.2008.
105312). PMID 18719199 (https://www.ncbi.nlm.nih.gov/pubmed/18719199).
63. Prolaktin (http://www.medical.siemens.com/siemens/en_GLOBAL/gg_diag_FBAs/files/referenzwerte_pdf/IMMULITE_
Systeme/prolaktin.pdf) Archived (https://web.archive.org/web/20110728085232/http://www.medical.siemens.com/sie
mens/en_GLOBAL/gg_diag_FBAs/files/referenzwerte_pdf/IMMULITE_Systeme/prolaktin.pdf) 28 July 2011 at the
Wayback Machine at medical.siemens.com—reference ranges as determined from the IMMULITE assay method
64. The AIA essay values are also from Table 2 (http://www.clinchem.org/cgi/content/full/54/10/1673/T2) in Beltran 2008,
like the other values, but it uses a different conversion factor of 27.0 mIU/L per µg/L, taken from the second
international standard, IS 83/562).
65. Melmed S, Kleinberg D 2008 Anterior pituitary. 1n: Kronenberg HM, Melmed S, Polonsky KS, Larsen PR, eds.
Willams textbook of endocrinology. 11th ed. Philadelphia: Saunders Elsevier; 185–261
66. Amir LH (2001). "Maternal smoking and reduced duration of breastfeeding: a review of possible mechanisms". Early
Human Development. 64 (1): 45–67. doi:10.1016/S0378-3782(01)00170-0 (https://doi.org/10.1016%2FS0378-3782%
2801%2900170-0). PMID 11408108 (https://www.ncbi.nlm.nih.gov/pubmed/11408108).
67. Amir LH, Donath SM (2002). "Does maternal smoking have a negative physiological effect on breastfeeding? The
epidemiological evidence". Birth (Berkeley, Calif.). 29 (2): 112–23. doi:10.1046/j.1523-536X.2002.00152.x (https://doi.
org/10.1046%2Fj.1523-536X.2002.00152.x). PMID 12000412 (https://www.ncbi.nlm.nih.gov/pubmed/12000412).
68. Coutts RT, Smail GA (12 May 2014). Polysaccharides Peptides and Proteins: Pharmaceutical Monographs (https://bo
oks.google.com/books?id=ojGRBQAAQBAJ&pg=PA153). Elsevier. pp. 153–. ISBN 978-1-4831-9612-1.
69. D.F. Horrobin (6 December 2012). Prolactin: Physiology and Clinical Significance (https://books.google.com/books?id
=h_Q-BAAAQBAJ&pg=PA13). Springer Science & Business Media. pp. 13–. ISBN 978-94-010-9695-9.
70. Martin H. Johnson (14 December 2012). Essential Reproduction (https://books.google.com/books?id=qXpBst5hJs0C
&pg=PT40). John Wiley & Sons. pp. 40–. ISBN 978-1-118-42388-2.
71. Jan Riordan (January 2005). Breastfeeding and Human Lactation (https://books.google.com/books?id=aiVesab_2bw
C&pg=PA468). Jones & Bartlett Learning. pp. 468–. ISBN 978-0-7637-4585-1.

External links
MedlinePlus Encyclopedia Prolactin (https://medlineplus.gov/ency/article/003718.htm)

Retrieved from "https://en.wikipedia.org/w/index.php?title=Prolactin&oldid=923097251"

This page was last edited on 26 October 2019, at 10:15 (UTC).


Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this
site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia
Foundation, Inc., a non-profit organization.

You might also like