Biomedical subjects

M Wendel

Publications and source records attributed to M Wendel.

30 records · Page 2Linked to original sources

PubMed1994

Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. Modulation of osteoclast adhesion in vitro.

The tartrate-resistant acid phosphatase (TRAP) of skeletal osteoclasts was found to partially dephosphorylate the bone matrix phosphoproteins osteopontin (OPN) and bone sialoprotein (BSP). TRAP also partially dephosphorylated metabolically [32P]PO4-labeled OPN as well as BSP, whereas comparable amounts of either alkaline phosphatase or prostatic acid phosphatase, at their respective pH optima, were ineffective, indicating a certain preference of TRAP for these phosphoprotein substrates. It has previously (Flores, M., Norgärd, M., Heinegård, D., Reinholt, F. P., and Andersson, G. (1992) Exp. Cell Res. 201, 526-530) been shown that osteoclasts bind to OPN as well as to BSP coated onto glass. We can now show that the partially dephosphorylated proteins no longer support osteoclast binding. These results indicate that the secretion of TRAP from osteoclasts into the resorption area could exert a regulatory influence on the attachment of the cells to the bone surface. This could imply roles in the development of ruffled borders and/or in the regulation of osteoclast motility on the bone surface.

Acid Phosphatase↗

PubMed1994

Distribution and synthesis of bone sialoprotein in metaphyseal bone of young rats show a distinctly different pattern from that of osteopontin.

Bone sialoprotein (BSP) and osteopontin (OPN) are two phosphorylated and highly glycosylated cell-binding proteins in bone. Both proteins bind to hydroxylapatite. The cell binding is mediated via an Arg-Gly-Asp (RGD) sequence and previous work indicates that both proteins can bind to the vitronectin receptor (alpha v beta 3). The present work shows that a prevailing localization of BSP in metaphyseal bone of the young rat is at the interface between calcified cartilage and bone. Thus BSP shows a conspicuous enrichment in the osteoid laid down by the invading osteoblasts immediately next to the calcified cartilage. Furthermore, the most prominent amount of BSP mRNA was detected in cells at the epiphyseal/metaphyseal border. As opposed to OPN, no prominent accumulation of BSP immunoreactivity was observed at bone surfaces that face cells. Also the synthesis OPN was most pronounced at sites very different from those of BSP. Thus, the most prominent amount of OPN mRNA was observed in cells close to the metaphyseal/diaphyseal border, where osteoclastic bone resorption is particularly active. Indeed, message was often found in cells surrounding osteoclasts without any detectable message. The distinctly different patterns of synthesis and expression of the two proteins indicate different roles in bone turnover at this stage of development. Thus, it appears that BSP has a specific role during the initial phases of bone formation at the cartilage/bone interface. On the other hand, the pattern of OPN synthesis and expression support and extend our previous data showing OPN particularly enriched at attachment sites of osteoclasts resorbing bone.

Amino Acid Sequence↗

PubMed1993

A major non-collagenous 62 kDa protein from rat bone mineralized matrix is identical to pp63 a phosphorylated glycoprotein from liver.

A protein present as a M(r) 62 k monomer and as several differently sized disulfide-bonded oligomers has been isolated from rat bone mineralized matrix. Its overall tissue distribution determined by ELISA immunoassays showed the protein present only in bone, tooth and in serum while aorta, cartilage, intestine, kidney, liver, muscle, skin, spleen and tendon were all negative. Despite that the 62 kDa protein was abundant and selectively found in bone, no positive cDNA clone could be identified in several rat bone libraries. Positive clones were, however, identified in a rat liver expression library. A cDNA clone of 1.3 kb hybridized in a Northern blotting assay to a 1.8 kb mRNA in rat liver. No hybridization signal was detected with RNA from bone, brain, lung, muscle, spleen and kidney. Sequence analysis of the isolated cDNA clone revealed a 50-bp untranslated region followed by an open reading frame of 357 amino acids. The open reading frame can be divided into a 17-amino acid signal peptide followed by the mature protein of 340 amino acids with alanine as its N-terminal amino acid. A short N-terminal amino acid sequence from the isolated 62-kDa bone protein verified the molecular identity of the cDNA clone. The primary structure of the 62-kDa liver protein was identical to a that of a 63-kDa phosphorylated glycoprotein (pp63) from liver.

Animals↗

PubMed1992

Cartilage matrix proteins. An acidic oligomeric protein (COMP) detected only in cartilage.

An Mr = 524,000 oligomeric protein was isolated from bovine cartilage and designated COMP (Cartilage Oligomeric Matrix Protein). The protein is composed of disulfide-bonded subunits with an apparent Mr of 100,000 each. It is markedly anionic, probably due to its high contents of aspartic acid and glutamic acid, as well as to its substitution with negatively charged carbohydrates. COMP was found in all cartilages analyzed, but could not be detected in other tissues by enzyme-linked immunosorbent assay of guanidine HCl extracts. Within a given cartilage, COMP shows a preferential localization to the territorial matrix surrounding the chondrocytes.

Amino Acids↗

PubMed1992

Regenerative response to membranous and enchondral lyophilized allogeneic bone in rabbit skull defects.

The regenerative responses of inlays of lyophilized allogeneic bone of membranous (skull) and enchondral (tibia) origin were studied in an experimental cranioplasty model in rabbits. The lyophilized bone particles were also bioassayed for inductive bone production in an orthotopic critical size defect rat model. Three trephined calvarial defects were evaluated in each of 14 adult rabbits. The experimental materials were implanted into two of the defects and the third was left empty for control purposes. The implants disclosed no major structural divergences as assessed by scanning electron microscopy. Healing was evaluated by light microscopy and contact radiography after periods of four and 15 weeks. The lyophilized bone allografts of both embryonic origins displayed a similar fashion of bone regeneration, bone marrow reappearance, and volumetric density of trabecular bone substance and displayed no obvious differences between experimental groups or intervals. The two materials exhibited low osteoinductive potential.

Animals↗

PubMed1991

Cartilage matrix proteins. A basic 36-kDa protein with a restricted distribution to cartilage and bone.

A non-collagenous quantitatively prominent protein was purified from guanidine hydrochloride extracts of bovine tracheal cartilage. Purification was achieved by cesium chloride density gradient centrifugation and chromatography on DEAE-cellulose at pH 7.0 followed by CM-cellulose at pH 5.0. The protein has a marked tendency to form aggregates in denaturing solutions of high ionic strength, e.g. 6 M guanidine hydrochloride. The purified protein contains a single, Mr 36,000 polypeptide chain, with a particularly high content of leucine. It contains about 1% carbohydrate with a remarkable absence of hexosamines and sialic acid, whereas xylose, galactose, mannose, and fucose were identified in the preparation. The protein was identified in extracts of cartilage and bone and could be shown to be primarily extracellular. Tendon may contain trace amounts of the protein, whereas extracts of several other tissues showed no immunoreactivity in enzyme-linked immunosorbent assay.

Animals↗

PubMed1991