Human hair keratins were among the first to be studied but it is only
recently that sufficient information has been obtained to gain a basic
biologic perspective of these proteins. Hair keratins are members of
the intermediate filament family of proteins, yet are sufficiently div
ergent from epidermal keratins to warrant separate classification: typ
e Ia and IIa (''hard''/hair keratins) and type Ib and IIb (epidermal a
nd other ''soft'' keratins). As with hair keratins from other species,
the human proteins may be distinguished from their epidermal counterp
arts by a relatively higher cysteine content, 7.6% versus 2.9%, respec
tively. This feature reflects utilization of disulfide bonding in prod
ucing a tougher, more durable structure in the tissues in which the ha
ir keratins are distributed. Although prominent in hair, their distrib
ution is not strictly limited to this tissue. A number of molecular ch
aracteristics have been elucidated from human hair keratin gene studie
s including amino acid sequence data for a type la hair keratin. Studi
es of various pedigrees has revealed a fairly wide latitude of variati
on in human hair keratin expression that is tolerated without associat
ed obvious hair phenotypic change. Thus, a foundation of knowledge reg
arding these proteins has emerged and continues to evolve.