Characterization of a unique collagenous fraction from limited pepsin digests of human placental tissue: molecular organization of the native aggregate

Furuto, Donald K.; Miller, Edward J.

doi:10.1021/bi00509a035

Cited by 50 publications

(29 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In particular, the fact that reduction and a second pepsin treatment of native short-chain collagen yield a uniform component, still containing all three chains in a shortened form in a nearly equimolar ratio, can hardly be explained without assuming that the three chains form one molecule. We were not ablc to confirm the results reported by Furuto and Miller [3] who separated, under nondenaturing conditions, a more acidic component containing one chain (corresponding to SC1) from a more basic one composed of two chains.…”

Section: Discussioncontrasting

confidence: 71%

Further Characterization of the Three Polypeptide Chains of Bovine and Human Short‐Chain Collagen (Intima Collagen)

Jander

Rauterberg

Glanville

1983

European Journal of Biochemistry

104

View full text Add to dashboard Cite

Short-chain collagen was isolated from bovine and from human placenta after limited pepsin digestion. By reductive cleavage of disulfide bonds under non-denaturing conditions, mainly non-collagenous domains were cleaved off yielding a uniform component composed of three polypeptide chains with molecular masses between 37 kDa and 48 kDa in a nearly equimolar ratio. The chains (SCI *, SC2* and SC3*) were isolated and characterized.By comparison of peptide patterns obtained after various cleavage procedures, they could be identified as more or less shortened forms of SCI, SC2 and SC3, the isolation of which from bovine short-chain collagen has been described [Jander et al. (1981) Eur. J . Biochem. 114,[17][18][19][20][21][22][23][24][25].The peptide patterns; as well as N-terminal sequence determination, give evidence for the genetic individuality of the three chains; the data so far available suggest that together they form one triple-helical structure which represents the collagenous domain of the basic molecular unit of short-chain collagen.A high-molecular-mass disulfide-bonded collagenous protein was first described by Chung et al. [I], who isolated it from aortic walls after limited pepsin digestion. Other authors used human [2,3] or bovine [4] placenta or calf skin [5] as a source for isolation. It represents a new and unique collagen type which, after reduction of disulfide bonds, releases three polypeptide chains of 40 -55 kDa, about half the size of the a chains of interstitial collagen types. We therefore introduced the term 'short-chain collagen'; because of its accumulated, though not exclusive, presence in the intima of vessel walls, it is also referred to as 'intima collagen'. Several chemical characteristics (amino acid composition, sugar content) demonstrate some similarity to typeIV and V collagens. With respect to the unusually high cysteine content, it closely resembles 7s collagen which has recently been identified as the cross-linking region of type IV collagen [6].In a previous paper [4] we described the isolation of three polypeptide chains SCI, SC2 and SC3 and some of their characteristic features. After the native aggregate has been reduced and alkylated under non-denaturing conditions, a second pepsin treatment leads to the loss of a larger noncollagenous portion of the molecule. Three shortened chains can be isolated from the remaining collagenous part. The characterization of these chains, described in this paper, provides evidence that three individual polypeptide chains are involved in the formation of short-chain collagen.

show abstract

Section: Discussioncontrasting

confidence: 71%

Further Characterization of the Three Polypeptide Chains of Bovine and Human Short‐Chain Collagen (Intima Collagen)

Jander

Rauterberg

Glanville

1983

European Journal of Biochemistry

104

View full text Add to dashboard Cite

show abstract

“…About 2300 nucleotides of the coding strand in the cDNA insert contain an open reading frame that can be translated into a polypeptide of 750 amino acid residues. As indicated in the text and at the top of the figure, the polypeptide sequence can be divided into three collagenous domains (COL 1-3) and four noncollagenous domains (NC [1][2][3][4]. As discussed in the text, we propose that the polypeptide encoded by pYN1738 represents one of the subunits of the collagen that gives rise to the proteolytic fragments HMW and LMW (17) after pepsin extraction of cartilage.…”

Section: Resultsmentioning

confidence: 99%

“…Thus, while type I collagen is the major collagen of bone, skin, tendons, and ligaments, type II collagen is found primarily in hyaline cartilage, and type IV collagen is the collagen of basement membranes. In addition, types III, V, VI, and VII collagens (1)(2)(3)(4)(5)(6)(7)(8)(9) show characteristic tissue distributions, which probably reflect their specific functions in different tissues.…”

mentioning

confidence: 99%

Synthesis and characterization of cDNA encoding a cartilage-specific short collagen.

Ninomiya¹,

Olsen²

1984

Proc. Natl. Acad. Sci. U.S.A.

125

View full text Add to dashboard Cite

Hyaline cartilage contains a unique set of collagenous proteins. Type II collagen is the most abundant, constituting about 85% of the total cartilage collagen. In addition, several minor collagenous components have been described. To study the structure and developmental regulation of chondrocyte-specific collagens, we have constructed a cDNA library from embryonic chicken sternal cartilage mRNA. We report here on the isolation and characterization of a 3200 base-pair-long cDNA that codes for a collagenous polypeptide of unusual structure in that the total length of the molecule is only about half of proal(ll) collagen chains. The mRNA for this polypeptide is considerably smaller than mRNA encoding the proa chains of interstitial collagens. In addition, the peptide encoded by the cDNA appears to contain at least three domains with triple-helical potential separated by short, noncollagenous peptides. Between the three collagenous domains are several cysteinyl residues.The collagens comprise a family of extracellular matrix proteins that are products of at least 10 different genes (for review, see ref. 1). Although these proteins all contain rigid, rod-like triple-helical domains, it is now recognized that they also exhibit extensive structural diversity. Although this diversity is in part due to variations in post-translational modifications of different collagens during their biosynthesis, it is first and foremost a consequence of variation in primary structure. Since there are tissue-specific differences in the expression of collagen types, it is generally assumed that this structural diversity is responsible for differences in the functional properties of various connective tissues. Thus, while type I collagen is the major collagen of bone, skin, tendons, and ligaments, type II collagen is found primarily in hyaline cartilage, and type IV collagen is the collagen of basement membranes. In addition, types III, V, VI, and VII collagens (1-9) show characteristic tissue distributions, which probably reflect their specific functions in different tissues.The chondrocyte population in cartilage synthesizes a unique set of collagenous proteins (10). Of these collagens, type II collagen, with molecules consisting of three identical al(II) chains, is the most abundant, constituting -85% of the total tissue collagen. In addition, hyaline cartilage contains several minor collagenous components. Among these are "G collagen" (also called "short-chain collagen"), isolated from chondrocyte cultures (11-14), and components identified in pepsin extracts of hyaline cartilage (15-21). To study the structure and developmental regulation of chondrocyte-specific collagens, we have constructed a cDNA library from 17-day chicken embryo sternal cartilage mRNA and screened it for cDNAs specific for collagenous polypeptides (22). In this report, we describe the isolation and characterization of a cDNA that codes for a collagenous polypeptide showing several unusual characteristics. First, the total length of the molecule is only ...

show abstract

“…Type v collagen was isolated by salt precipitation from pepsin digests of human uterine cervical tissues by the methods described elsewhere (19,20). the extracted type V collagen was also lyophilized.…”

Section: Methodsmentioning

confidence: 99%

Decreased type III collagen expression in human uterine cervix of prolapse uteri

Iwahashi

Muragaki

2011

Experimental and Therapeutic Medicine

View full text Add to dashboard Cite

Abstract. the precise mechanism of prolapse uteri is not fully understood. there is evidence to suggest that abnormalities of collagen, the main component of extracellular matrix, or its repair mechanism, may predispose women to prolapse. to investigate the characteristic structure of human uterine cervix of patients with prolapse uteri, various types of collagen expression in the uterine cervix tissues of the prolapse uteri were compared to those of normal uterine cervix. after informed consent, 36 specimens of uterine cervical tissues were obtained at the time of surgery from 16 postmenopausal women with prolapse uteri (stage iii-iV by the pelvic Organ Prolapse Quantification examination) and 20 postmenopausal women without prolapse uteri (control group). Collagens were extracted from the uterine cervix tissues by salt precipitation methods. the relative levels of various collagens were evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. the uterine cervix was longer in the patients with prolapse uteri than those of postmenopausal controls without prolapse uteri. the ratios of type iii to type i collagen in the uterine cervical tissues were significantly decreased in the prolapse uteri, as compared to those of the postmenopausal uterine cervix without prolapse. these results suggest that decreased type iii collagen expression may play an important role in determing the physiology and structure of the uterine cervix tissues of prolapse uteri. IntroductionThe extracellular matrix (ECM) is considered to play an important role in the stability of tissues and in regulating the growth and differentiation of cells (1,2). Synthesis, accumulation and catabolism of the Ecm occur during wound healing and during the initiation and progression of numerous diseases (3). moreover, it is generally acknowledged that the Ecm does not function as a mere passive scaffold for connective tissue within organ architecture. it also plays an 'informational' role through a network of interactions between cells and signal molecules which is of primary importance in the control of cellular proliferation and motility during histogenesis for the maintenance of tissue homeostasis and in cancer development.prolapse of the pelvic organs is a common disease affecting the lives of millions of women. Women with prolapse suffer from chronic pelvic pain and pressure, urinary and fecal incontinence, sexual dysfunction and social isolation. despite the high prevalence of this disease and the devastating impact on the lives of women, very little is known about its pathophysiology.recently, it has been suggested that a structural defect in the vagina and its supportive tissues, such as a decrease in collagen content or a change in collagen subtypes, is one of the mechanisms that predisposes a woman to prolapse. thus, there have been many studies throughout the literature in which collagen is analyzed in vaginal and uterine-supporting ligament biopsies procured at the time of a repair of prolapse in patients with prolapse or at the t...

show abstract

Characterization of a unique collagenous fraction from limited pepsin digests of human placental tissue: molecular organization of the native aggregate

Cited by 50 publications

References 10 publications

Further Characterization of the Three Polypeptide Chains of Bovine and Human Short‐Chain Collagen (Intima Collagen)

Further Characterization of the Three Polypeptide Chains of Bovine and Human Short‐Chain Collagen (Intima Collagen)

Synthesis and characterization of cDNA encoding a cartilage-specific short collagen.

Decreased type III collagen expression in human uterine cervix of prolapse uteri

Contact Info

Product

Resources

About