Isolation and characterization of a collagen-binding glycoprotein from chondrocyte membranes.

Mollenhauer, Jürgen; Mark, Klaus von der

doi:10.1002/j.1460-2075.1983.tb01378.x

Cited by 142 publications

(68 citation statements)

References 39 publications

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“…* Chicken annexin V (anchorin CII) was o~~nally isolated from chondrocyte membranes by aBinity chromatography on native collagen type II [12,13]. In contrast to annexin II which remains strictly intracellular [14], annexins I and V are also secreted from cells by a yet unknown mechanism, although the proteins contain neither a signal peptide nor a transm~brane sequence [15,16].…”

Section: Introductionmentioning

confidence: 99%

Organisation of the chicken annexin V gene and its correlation with the tertiary structure of the protein

et al. 1993

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Chicken annexin V (anchorin CII) is a collagen binding, membrane-associated molecule with Ca" channel activity. Here we report on the coding sequences, promotor region, size and distribution of exons, and exon-intron junctions of the chicken annexin V gene. It is about 25 kb long and codes for 13 short exons between 50 and 581 bp length. Exon sizes and locations of splice sites are almost completely homologous to those of the human and mouse annexin II or pigeon annexin I genes, although there is only SO-60% homology in the sequence of the corresponding proteins. The four repeat structure and symmetry of the armexin V as evident from sequence and X-ray analysis studies is only partially reflected in this highly conserved exon dist~bution. In the first two repeats of chicken annexin V the exons correlate with protein domains ~n~ining one, two, or three a-helices, while in the repeats 3 and 4 exon junctions and o-helical domains do not correlate. The analysis of the promotor structure revealed the absence of a typical TATA-box, but a GC-rich region which may possibly promote transcription from several start sites.

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Section: Introductionmentioning

confidence: 99%

Organisation of the chicken annexin V gene and its correlation with the tertiary structure of the protein

et al. 1993

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“…l ; see also [22]). The titer of the antiserum was determined by ELISA on microtiter plates coated with either whole chondrocyte membranes or purified anchorin CII (Table I).…”

Section: Preparation Of Antibodies Directed Against Anchorin Cllmentioning

confidence: 84%

“…Preparation ofAnti-anchorin Cll Antiserum : AnchorinCIlwas purified by affinity chromatography on type II collagen Sepharose of Nonidet-P40-solubilized chondrocyte membranes as described previously (22). The resultant protein is pure by criteria of SDS gel electrophoresis after silver staining (23) (Fig.…”

Section: Methodsmentioning

confidence: 99%

“…Frozen sections from either 16-d embryonic chick tibia or sternum were pretreated with testicular hyaluronidase to re- FIGURE 1 Silver stained SDS PAGE of chondrocyte membranes (a) and purified anchorin CII (b), isolated from chick chondrocyte plasma membranes by affinity chromatography on type II collagen sepharose (22) . Values at right represent the molecular weight x 10 -3 .…”

Section: Localization Of Anchorin Cll In Cartilage Tissuementioning

confidence: 99%

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Role of anchorin CII, a 31,000-mol-wt membrane protein, in the interaction of chondrocytes with type II collagen.

Mollenhauer¹,

Bee²,

Lizarbe³

et al. 1984

The Journal of Cell Biology

132

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We have previously reported the isolation of a hydrophobic, type-II Collagenbinding glycoprotein of molecular weight 31,000 (31,000-mol-wt protein) from chick chondrocyte membranes (Mollenhauer, J ., and K. von der Mark, EMBO Eur. Mol. Biol. Organ . l., 2 :45-50) . The function of this protein in anchoring pericellular type II collagen to the chondrocyte surface was inferred from its ability to bind native type-II collagen either when detergent solubilized or when inserted into liposomes . In the present study we have used specific antibodies to localize this protein, which we now call anchorin CII, to the surface of chondrocytes in both cartilage sections, and in cell culture . In immunofluorescence studies of isolated chondrocytes we observed a dense, punctate distribution of anchorin CII on the cell surface when chondrocytes were enclosed by a pericellular type II collagen matrix . Removal of the pericellular matrix with trypsin also removed anchorin CII . The membrane protein character of anchorin CII was indicated by the demonstration of antibody-induced patching and capping on the chondrocyte surface at 22°C and 37°C, respectively . In monolayer culture, the amount of anchorin CII appeared reduced on flattened chondrocytes lacking a pericellular type II Collagen matrix but was prominent upon intercellular cell processes . Fab' fragments prepared from either anchorin CII antiserum or an antiserum directed against the entire chondrocyte membrane inhibited the attachment of chondrocytes to a type II collagen substrate . In each case, the inhibition of attachment was neutralized by preincubation of Fab' fragments with purified anchorin CII .In hyaline cartilage, chondrocytes are embedded in an extracellular matrix consisting predominantly of chondroitin sulfate proteoglycan, type II collagen, several minor collagens, and glycoproteins. Type II collagen represents about 80-90% of the total cartilage collagen (1, 2). Minor cartilage collagens include molecules consisting of la, 2a, and 3a chains (3) and a class of collagen fragments characterized by intramolecular cystine bridges, M-collagens (4-7); they represent about 10-15% of the cartilage collagen (for review see reference 8).Collagen provides the three-dimensional framework of the cartilage matrix in which the proteoglycans are imbedded and contributes essentially to the mechanical and physiological properties of cartilaginous tissues . However, type II collagen has also been shown to be influential in chondrogenic differentiation (9-12), and in the regulation of the chondrocyte phenotype (for review see 13,14) .Immunohistochemical and clectronmicroscopical studies on isolated chondrocytes (15)(16)(17)(18)(19) have demonstrated a close association of type II collagen with the chondrocyte surface . The precise nature ofthis cell:matrix association, however, is still unclear . Chondronectin, an adhesion factor that enhances 1572 the binding of chondrocytes to a collagen substrate, has been isolated from serum (20,21). Whether this component is intim...

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“…Its anti-inflammatory, anticoagulant and growth-inhibitory actions stem from diverse properties that include calcium ion channel activity [1], inhibition of signal transduction enzymes, such as protein kinase C and phospholipase A # [2,3], avid calcium-dependent binding to anionic membrane phospholipids [4] or cytosolic protein targets [5], and interaction with extracellular matrix proteins [6][7][8]. Annexin A5 is abundantly and ubiquitously expressed [9], and is further inducible by phorbol esters [10], the c-fos oncogene [11], oestradiol [12] and gonadotropin-releasing hormone [13].…”

Section: Introductionmentioning

confidence: 99%

Functional analysis of the human annexin A5 gene promoter: a downstream DNA element and an upstream long terminal repeat regulate transcription

Carcedo

Iglesias

Bances

et al. 2001

Biochemical Journal

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Human annexin A5 is a ubiquitous protein implicated in diverse signal transduction processes associated with cell growth and differentiation, and its gene regulation is an important component of this function. Promoter transcriptional activity was determined for a wide 5′ portion of the human annexin A5 gene, from bp −1275 to +79 relative to the most 5′ of several discrete transcription start points. Transfection experiments carried out in HeLa cells identified the segment from bp −202 to +79 as the minimal promoter conferring optimal transcriptional activity. Two canonical Sp1 sites in the immediate 5′ flanking region of a CpG island were required for significant transcription. Strong repressive activity in the distal promoter region between bp −717 to −1153 was attributed to the presence of an endogenous retroviral long terminal repeat, homologous with long terminal repeat 47B. The downstream sequence from bp position +31 to +79 in untranslated exon 1 was also essential for transcription, as its deletion from any of the plasmid constructs abolished activity in transfection assays. Electrophoretic mobility-shift assays, Southwestern-blot analysis and affinity chromatography were used to identify a protein doublet of relative molecular mass 35kDa that bound an octanucleotide palindromic sequence in exon 1. The DNA cis-element resembled an E-box, but did not bind higher molecular mass transcription factors, such as upstream stimulatory factor or activator protein 4. The discovery of a downstream element crucial for annexin A5 gene transcription, and its interaction with a potentially novel transcription factor or complex, may provide a clue to understanding the initiation of transcription by TATA-less, multiple start site promoters.

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Isolation and characterization of a collagen-binding glycoprotein from chondrocyte membranes.

Cited by 142 publications

References 39 publications

Organisation of the chicken annexin V gene and its correlation with the tertiary structure of the protein

Organisation of the chicken annexin V gene and its correlation with the tertiary structure of the protein

Role of anchorin CII, a 31,000-mol-wt membrane protein, in the interaction of chondrocytes with type II collagen.

Functional analysis of the human annexin A5 gene promoter: a downstream DNA element and an upstream long terminal repeat regulate transcription

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