Localization of low-sulfur keratin proteins in the wool follicle using monoclonal antibodies

نویسندگان

  • P W French
  • D R Hewish
چکیده

Monoclonal antibodies that recognize components of the low-sulfur keratin proteins extracted from Merino wool have been used to locate these components within the wool follicle. Immunoblotting procedures showed that all of the monoclonal antibodies bound more than one of the eight low-sulfur protein components, indicating that these proteins have antigenic determinants in common. Immunofluorescence studies showed that those antibodies specific for the component 7 family of the low-sulfur proteins bound to the developing wool fiber, whereas those antibodies recognizing the component 8 family bound to areas throughout the wool follicle, particularly the inner and outer root sheaths, but also to the fiber, the cuticle, and the epidermis. One of the monoclonal antibodies also bound to intermediate filament networks of cultured human epithelial cells.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Structure and expression of genes for a class of cysteine-rich proteins of the cuticle layers of differentiating wool and hair follicles

The major histological components of the hair follicle are the hair cortex and cuticle. The hair cuticle cells encase and protect the cortex and undergo a different developmental program to that of the cortex. We report the molecular characterization of a set of evolutionarily conserved hair genes which are transcribed in the hair cuticle late in follicle development. Two genes were isolated an...

متن کامل

Incorporation of [Me-3H]methionine into wool follicle proteins: a biochemical and ultrastructural study.

The formation of the 'low-sulphur' group of proteins which constitutes more than half the cortical cell content of wool was investigated. Of the amino acids present in the lowand highsulphur proteins isolated from wool, methionine is the only one which is exclusive to the low-S group. The incorporation of [Me-'H]methionine, administered intradermally to a sheep, was examined using both biochemi...

متن کامل

Acidic and basic hair/nail ("hard") keratins: their colocalization in upper cortical and cuticle cells of the human hair follicle and their relationship to "soft" keratins

Although numerous hair proteins have been studied biochemically and many have been sequenced, relatively little is known about their in situ distribution and differential expression in the hair follicle. To study this problem, we have prepared several mouse monoclonal antibodies that recognize different classes of human hair proteins. Our AE14 antibody recognizes a group of 10-25K hair proteins...

متن کامل

Distribution of prolactin receptor immunoreactivity in ovine skin and changes during the wool follicle growth cycle.

Prolactin is believed to mediate seasonal cues entraining seasonal reproductive and hair follicle growth cycles. Prolactin receptor binding activity and prolactin receptor gene expression in mammalian skin have recently been described. In this report, prolactin receptor immunoreactivity is identified in sheep skin using a monoclonal antibody against the rat liver prolactin receptor. Western blo...

متن کامل

In Vitro Assembly and Structure of Trichocyte Keratin Intermediate Filaments

Intermediate filaments (IF) have been recognized as ubiquitous components of the cytoskeletons of eukaryotic cells for 25 yr. Historically, the first IF proteins to be characterized were those from wool in the 1960s, when they were defined as low sulfur keratins derived from "microfibrils." These proteins are now known as the type Ia/type IIa trichocyte keratins that constitute keratin IF of se...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of Cell Biology

دوره 102  شماره 

صفحات  -

تاریخ انتشار 1986