Lec.

3 Histochemistry
 Epidermal Appendages
1. HAIR
❑Elongated keratinized structures for keratinocytes matrix to form in hair
follicles , (central medulla, which surrounded by cortex, which surrounded by
cuticle ).
❑Melanocytes in the hair bulb matrix transfer melanosomes into the epithelial
cells that will later differentiate to form the hair.
❑Each hair has hair shaft (outside of skin surface), hair root (the medial part )
and hair bulb (deeper part).
❑Dermal hair papilla penetrates the base of the hair bulb, and its vasculature
supplies nutrients and O 2 for proliferating and differentiating cells.
❑The growing hair root is surrounded by internal and external root sheaths of
the epidermis and a connective tissue sheath.
I. Shaft
II. Root
III. Hair bulb

Hair follicle

Provides hair
with nutrition
 Note
➢Straight hair are stronger than curly hair.
➢Hair do not grow continuously but have a growth cycle (three major
phases):
1) Anagen: long period of mitotic activity and growth.
2) Catagen: A brief period of arrested growth and regression of the
hair bulb.
3) Telogen: A final long period of inactivity during which the hair may
be shed.
➢Growth rate of hair is approximately 1.5–2.2 mm per week.
➢ Life span of hair varies from region to region; in scalp (4 years), in
axilla (4 months).
 Hair disorders
➢Greying or whitening of hair is caused by either
failure of melanocytes to form pigment granules.
➢Baldness is caused by progressive atrophy of
hair follicle with age, genetic factor or presence
of androgenic hormone.
➢ Alopecia due to autoimmune disorder: Alopecia
areata hair loss in patches Alopecia universalis:
loss of all body hair.
Chemical structure of human hair
2. NAILS
❑Nails are a cornified plate (hard keratin)
of stratum corneum found on the dorsal
surface of the terminal part of fingers
and toes, they formed by keratinization
process starts in nail root then growing
nail plate with edges covered by skin
folds.
❑The growth rate about 3 mm/mo. for
fingernails and 1 mm/mo. for toenails.
 ‫هم‬
3. Glands of skin ‫م‬
Skin includes three major types of exocrine glands:
➢Eccrine (Merocrine) sweat glands in the dermis produce sweat (by
exocytosis via duct, no part of the gland is lost or damaged) that is
mostly water onto the skin surface for cooling the body.
➢ Apocrine sweat glands by membrane budding (loss of cytoplasm) and
secrete protein-rich sweat onto the hair of hair follicles (Apocrine
gland has less damage than holocrine secretion). ‫الماده الزيتية‬
➢Sebaceous glands produce sebum by holocrine secretion (by ‫حول الشعر‬
membrane rupture), secreting this oily substance onto hair in the
follicles (Note: pilosebaceous unit = Hair follicle + Sebaceous gland).
Connective Tissue (extracellular matrix (ECM))
I. Ground substance and II. Protein fibers.

I. Ground Substance:
➢Its function as a viscous substance:
(1)Allows diffusion of small molecules
(2) Acts as both a lubricant and a barrier to the penetration of invaders.
➢The ground substance of ECM is a complex mixture of three major
kinds of macromolecules:
1). glycosaminoglycans (GAGs).
2) proteoglycans.
3) multiadhesive glycoproteins.
1. GAGs (also called mucopolysaccharides)

➢a. long polymer and most ubiquitous GAG

‫توجد عند‬
is hyaluronan (hyaluronic acid) (100s to ‫المفاصل‬
‫للتزييت‬
1000s of kDa) synthesized directly into the
ECM by an enzyme located in the cell
membrane of many cells.
➢b. All other GAGs are much smaller (10-40
kDa), sulfated, bound to proteins (as parts
of proteoglycans), where the four major
GAGs found in proteoglycans are
dermatan sulfate, chondroitin sulfates,
keratan sulfate, and heparan sulfate.
2. Proteoglycans
❑ They are consisting of a core protein to which are heavily glycosylated, which are a major
component of the animal extracellular matrix between cells.
❑ they are synthesized in the Golgi apparatus and become bound to the hyaluronan by link
proteins and their GAG side-chains associate further with collagen fibers and other ECM
component.
❑ Proteoglycans complex may link to very long hyaluronan molecules, and each proteoglycan
monomer has a core protein with a few or many side chains of the sulfated GAGs
Proteoglycans types:
(1) Perlecan (470 kDa): is a key component of the extracellular matrix of cartilage, where it is
essential for long bone growth
(2) Aggrecan (250 kDa): It is a critical component for cartilage structure.
(3) Decorin (140 kDa) which helps in fibrillogenesis
(4) Syndecan as a growth-factor-receptor activation and cell–cell adhesion, the syndecans
are 31, 20, 38, and 20 kDa in size, respectively
Many of proteoglycans bind and sequester various growth factors and other signaling
proteins.
❖ Note: Glycosylation: is the reaction in which a carbohydrate is attached to a
hydroxyl or other functional group by enzyme-catalysed reaction. Glycation: non-
enzymatic glycosylation.
3. Multiadhesive Glycoproteins
❑all have multiple binding sites for cell surface integrins and for other matrix macromolecules
with branched oligosaccharide chains and allow adhesion of cells to their substrate.
❑An example is the large (200-400 kDa), trimeric glycoprotein laminin with binding sites for
integrins, type IV collagen, and specific proteoglycans, providing adhesion for epithelial and
other cells.
❑Another glycoprotein, fibronectin is a 235-270 kDa dimer synthesized largely by fibroblasts,
with binding sites for collagens and certain GAGs, and forms insoluble fibrillar networks
throughout connective tissue.
II. Protein Fibers

❑Thay are elongated structures formed from proteins that polymerize after
secretion from fibroblasts.
❑The three main types of fibers include (1) Collagen, (2) Reticular,
(3) Elastic fibers.