Isolation from bovine elastic tissues of collagen type VI and characterization of its form in vivo.

نویسندگان

  • S Ayad
  • C A Chambers
  • C A Shuttleworth
  • M E Grant
چکیده

Foetal-bovine nuchal ligament and aorta, together with adult-bovine aorta and pregnant uterus, were extracted under dissociative conditions in the absence and in the presence of a reducing agent. A collagenous glycoprotein of Mr 140000 [designated component 140K(VI)], identified in these extracts as the major periodate/Schiff-positive component, was shown to be related to collagen type VI. Digestion of non-reduced extracts with pepsin yielded periodate/Schiff-positive peptides that, on the basis of their electrophoretic mobilities, amino acid analyses and peptide 'maps', were identical with type VI collagen fragments prepared by standard procedures. It is concluded that collagen type VI occurs in vivo as molecule comprising three chains of Mr 140000 in which the helical domains account for about one-third of each polypeptide. Biosynthetic experiments with nuchal-ligament fibroblasts in culture demonstrated that a bacterial-collagenase-sensitive [3H]fucose-labelled glycoprotein, Mr 140000, was immunoprecipitated from culture medium by a specific antibody to the pepsin-derived form of collagen type VI. This result suggests that the collagenous polypeptides [140K(VI) components] represent the biosynthetic precursors of type VI collagen that do not undergo processing to smaller species before deposition in the extracellular matrix. Analyses of 5M-guanidinium chloride extracts of tissues with markedly different elastin contents and at different stages of development suggested that there was no relationship between collagen type VI and elastic-fibre microfibrils, a conclusion supported by the observation that the immunoprecipitated glycoprotein, Mr 140000, was distinct from the glycoprotein MFPI, Mr 150000, believed to be a constituent of these microfibrils [Sear, Grant & Jackson (1981) Biochem. J. 194, 587-598].

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

Isolation and ultrastructural analysis of microfibrillar structures from foetal bovine elastic tissues. Relative abundance and supramolecular architecture of type VI collagen assemblies and fibrillin.

Extensive intact assemblies of matrix macromolecules have been solubilized from foetal calf skin, nuchal ligament and aorta by a new procedure that includes bacterial collagenase digestion under non-reducing, non-denaturing conditions and gel filtration chromatography. Type VI collagen was identified as the major microfibrillar element of these tissues by SDS-PAGE analysis and Western blotting....

متن کامل

Research Article: Isolation, characterization and biocompatibility evaluation of collagen from Thunnus tonggol skin

Acid-soluble collagen could be isolated from fish skin using acetic acid. In recent years, much attention has been paid to collagen from marine sources, mainly arising from the fact that there is no risk of contagious diseases. Moreover, by processing the fish, significant amounts of waste materials are produced which can be considered as a substitute for these collagen sources. Thunnus tonggol...

متن کامل

Type VI collagen microfibrils: evidence for a structural association with hyaluronan

Type VI collagen, a widespread structural component of connective tissues, has been isolated in abundance from fetal bovine skin by a procedure involving bacterial collagenase digestion under nonreducing, nondenaturing conditions and gel filtration chromatography. Rotary shadowing electron microscopic analysis revealed that the collagen VI was predominantly in the form of extensive intact micro...

متن کامل

Isolation and characterization of acid-soluble collagen from the skin of Rutilus Frisii Kutum (Kamensky) of the Caspian Sea

This study proceeds to extract collagen from the skin of Rutilus  kutum, one of  the main and economical species of the Caspian Sea. Acid-soluble collagen (ASC) from the skin of R. kutum was extracted and characterized by SDS-PAGE, FTIR and UV spectrophotometry. Based on the data from the SDS-PAGE and the composition of amino acid, it was probable that the obtained collagen classified as type I...

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 Biochemical journal

دوره 230 2  شماره 

صفحات  -

تاریخ انتشار 1985