Matrix (Stuttgart, Germany)最新文献_第9页

The serine proteinase inhibitory proteins of the human intervertebral disc: Their isolation, characterization and variation with ageing and degeneration 人椎间盘丝氨酸蛋白酶抑制蛋白:它们的分离、特征和随年龄和退变的变化

Matrix (Stuttgart, Germany) Pub Date : 1992-12-01 DOI: 10.1016/S0934-8832(11)80090-9

James Melrose , Peter Ghosh , Thomas K.F. Taylor , John L. Andrews

{"title":"The serine proteinase inhibitory proteins of the human intervertebral disc: Their isolation, characterization and variation with ageing and degeneration","authors":"James Melrose , Peter Ghosh , Thomas K.F. Taylor , John L. Andrews","doi":"10.1016/S0934-8832(11)80090-9","DOIUrl":"10.1016/S0934-8832(11)80090-9","url":null,"abstract":"<div><p>Serine proteinase inhibitory proteins (SPIs) were extracted from human disc tissues using 2 M GuHCl and subjected to CsCl density gradient ultracentrifugation. The SPIs recovered in the low buoyant density fractions (ϱ ≤ 1.35 g/ml) were purified by a combination of gel-permeation, ion-exchange, trypsin affinity, and reverse-phase high performance chromatographies. Characterisation of the major disc SPI by polyacrylamide gel electrophoresis, isoelectric focussing, enzyme inhibition and pH stability studies indicated that this small molecular weight (12–14 kDa), highly basic (pI > 9.5), acid-stable but alkaline-labile protein possessed potent inhibitory activity against bovine pancreatic trypsin and chymotrypsin, and human leukocyte elastase and cathepsin G. Two-major and two-minor low molecular weight cationic SPI species were identified by reverse-phase HPLC. The predominant species was identical to a human articular cartilage SPI sharing amino terminal sequence homology with the mucus proteinase inhibitors (MPIs). It also cross-reacted with an antiserum to the MPIs and behaved identically to secretory leucocyte proteinase inhibitor (SLPI) when examined by reverse phase HPLC, and SDS PAGE. A higher molecular weight (54 kDa), anionic (pI ∼ 4.6) SPI was also purified and identified as α<sub>1</sub>-proteinase inhibitor (α<sub>1</sub>-PI). Quantification of α<sub>1</sub>-PI and the small molecular weight cationic disc inhibitors indicated that the latter were depleted in morphologically degenerate disc tissues while levels of α<sub>1</sub>-PI were somewhat higher although a large proportion of the α<sub>1</sub>-PI was inactive. A depletion of total SPI levels was evident overall in degenerate discs suggesting a functional role for these inhibitory proteins in the maintenance of IVD matrix homeostasis.</p></div>","PeriodicalId":77253,"journal":{"name":"Matrix (Stuttgart, Germany)","volume":"12 6","pages":"Pages 456-470"},"PeriodicalIF":0.0,"publicationDate":"1992-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0934-8832(11)80090-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12462325","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 20

Authors Index 作者索引

Matrix (Stuttgart, Germany) Pub Date : 1992-12-01 DOI: 10.1016/S0934-8832(11)80096-X

引用次数: 0

Self-aggregation of squid cranial cartilage proteoglycans 鱿鱼颅软骨蛋白聚糖的自聚集

Matrix (Stuttgart, Germany) Pub Date : 1992-12-01 DOI: 10.1016/S0934-8832(11)80086-7

Demitrios H. Vynios , Matthias Mörgelin , Constantine P. Tsiganos

引用次数: 5

Verapamil decreases cyclic load-induced calcium incorporation in ROS 17/2.8 osteosarcoma cell cultures 维拉帕米降低ROS 17/2.8骨肉瘤细胞培养中循环负荷诱导的钙掺入

Matrix (Stuttgart, Germany) Pub Date : 1992-12-01 DOI: 10.1016/S0934-8832(11)80088-0

George P. Vadiakas , Albert J. Banes

{"title":"Verapamil decreases cyclic load-induced calcium incorporation in ROS 17/2.8 osteosarcoma cell cultures","authors":"George P. Vadiakas , Albert J. Banes","doi":"10.1016/S0934-8832(11)80088-0","DOIUrl":"10.1016/S0934-8832(11)80088-0","url":null,"abstract":"<div><p>Bone is a tissue that responds to mechanical load by changing its internal architecture. However, the mode of transmission of mechanical stimuli into biological signals and the effect of load at the cellular level are still not clear. An <em>in vitro</em> system, a Flexercell® Strain Unit, was used to apply cyclic load to osteoblast-like cells in culture. In the first series of experiments, ROS 17/2.8 rat osteosarcoma cells, cultured on Flex I®, flexible bottomed culture plates, were subjected to a 0.05 Hz, 0.24 STRAIN cyclic load regime for 3 and 7 days, <em>in vitro</em>. One group subjected to load received verapamil, a calcium channel blocker, throughout the experimental period. A second group was exposed to load but received no verapamil. A third group had no drug or load and a fourth group had no load but received verapamil. Cultures were incubated for 24 hours prior to collection with 10 μCi of <sup>45</sup>CaCl in the medium, then well bottoms were divided to yield outer (maximum) and inner (minimum) load zones for assay of radioactivity. The effect of verapamil during a 7-day loading period was studied by adding the drug to individual cultures at daily intervals. Results indicated that mechanical loading stimulates calcium incorporation in ROS 17/2.8 cell cultures by day 7 but not by day 3. Only early verapamil addition decreased load-induced calcium incorporation when drug was added prior to day 4. If verapamil was added after 4 days, the channel blocker did not diminish load-induced calcium incorporation.</p></div>","PeriodicalId":77253,"journal":{"name":"Matrix (Stuttgart, Germany)","volume":"12 6","pages":"Pages 439-447"},"PeriodicalIF":0.0,"publicationDate":"1992-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0934-8832(11)80088-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12462323","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 43

Initiation of Bone Regeneration in Adult Baboons by Osteogenin, a Bone Morphogenetic Protein 骨形成蛋白成骨素对成年狒狒骨再生的启动作用

Matrix (Stuttgart, Germany) Pub Date : 1992-11-01 DOI: 10.1016/S0934-8832(11)80033-8

U. Ripamonti , S. Ma , N.S. Cunningham , L. Yeates , A.H. Reddi

{"title":"Initiation of Bone Regeneration in Adult Baboons by Osteogenin, a Bone Morphogenetic Protein","authors":"U. Ripamonti , S. Ma , N.S. Cunningham , L. Yeates , A.H. Reddi","doi":"10.1016/S0934-8832(11)80033-8","DOIUrl":"10.1016/S0934-8832(11)80033-8","url":null,"abstract":"<div><p>Osteogenin, and related bone morphogenetic proteins, induce endochondral bone differentiation through a cascade of events which include formation of cartilage, hypertrophy and calcification of the cartilage, vascular invasion, differentiation of osteoblasts, and formation of bone. These events have been studied in a postnatal model of bone development in rodents. Information concerning the morphogenetic potential of osteogenin in primates is a prerequisite for potential clinical application in man. The efficacy of allogeneic osteogenin in primates was investigated in both extraskeletal and skeletal sites in 19-Chacma baboons (Papio ursinus). Osteogenin was isolated from demineralized baboon bone matrix and purified by chromatography on heparin-Sepharose, hydroxyapatite, and Sephacryl S-200. Protein fractions with a molecular mass range of 26-42 kDa induced cartilage and bone differentiation in the subcutaneous space of rats. Final purification to homogeneity was obtained by electroendosmotic elution from a preparative sodium dodecyl sulphate (SDS) polyacrylamide gel, resulting in a single band on a SDS-polyacrylamide gel with an apparent molecular mass of 30-34 kDa, with biological activity in rats. The osteoinductive potential of osteogenin in primates was tested first in intramuscular sites in baboons and found to be active. The bone regeneration potential was investigated in nonhealing calvarial defects surgically prepared in adult male baboons. Baboon osteogenin induced complete regeneration of the cranial wound. These findings in adult primates establish a primary role for osteogenin in initiation and promotion of osteogenesis; and imply a potential therapeutic application based on cell biology of extracellular matrix-cell interactions.</p></div>","PeriodicalId":77253,"journal":{"name":"Matrix (Stuttgart, Germany)","volume":"12 5","pages":"Pages 369-380"},"PeriodicalIF":0.0,"publicationDate":"1992-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0934-8832(11)80033-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12655011","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 104

A substrate-gel assay for hyaluronidase activity 透明质酸酶活性的底物-凝胶试验

Matrix (Stuttgart, Germany) Pub Date : 1992-11-01 DOI: 10.1016/S0934-8832(11)80035-1

Markus W. Guntenhöner , M. Anthony Pogrel , Robert Stern

引用次数: 99

Type X Collagen is Transcriptionally Activated and Specifically Localized During Sternal Cartilage Maturation X型胶原蛋白在胸骨软骨成熟过程中被转录激活并特异性定位

Matrix (Stuttgart, Germany) Pub Date : 1992-11-01 DOI: 10.1016/S0934-8832(11)80037-5

Phyllis Luvalle , Karla Daniels , Elizabeth D. Hay , Bjorn R. Olsen

{"title":"Type X Collagen is Transcriptionally Activated and Specifically Localized During Sternal Cartilage Maturation","authors":"Phyllis Luvalle , Karla Daniels , Elizabeth D. Hay , Bjorn R. Olsen","doi":"10.1016/S0934-8832(11)80037-5","DOIUrl":"10.1016/S0934-8832(11)80037-5","url":null,"abstract":"<div><p>Type X collagen is an extracellular matrix protein which is synthesized by chondrocytes when they undergo hypertrophy. We present evidence here that the expression of type X collagen in the developing chick sternum is controlled primarily by transcriptional mechanisms. Using chondrocyte nuclei isolated from 15-,16-,17- and 18-day chick embryonic sterna, nuclear run-off assays demonstrate that type X collagen gene transcription begins at day 16 in chondrocytes isolated from the cephalic portion. This occurs two days prior to mineralization of this tissue as observed by alizarin red staining. The rate of type X transcription increases dramatically through days 17 and 18. Western blot analyses of extracts of freshly isolated sternal chondrocytes from the same stages show that intracellular levels of the type X protein follow the same time course. Immunostaining with a monoclonal antibody specific for type X collagen demonstrates that the initial appearances of hypertrophic cells and pericellular type X collagen occur at embryonic day 16 in the cephalic portion of sterna. Observation of immunostained cephalic sternal sections from day 18 embryos by confocal microscopy reveals that type X collagen is localized in a capsule-like configuration around each hypertrophic chondrocyte.</p></div>","PeriodicalId":77253,"journal":{"name":"Matrix (Stuttgart, Germany)","volume":"12 5","pages":"Pages 404-413"},"PeriodicalIF":0.0,"publicationDate":"1992-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0934-8832(11)80037-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12654229","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 47

Type IV Collagen Synthesis and Accumulation in Neonatal Rat Aortic Smooth Muscle Cell Cultures 新生大鼠主动脉平滑肌细胞培养中IV型胶原的合成和积累

Matrix (Stuttgart, Germany) Pub Date : 1992-11-01 DOI: 10.1016/S0934-8832(11)80031-4

Ann C. Hospelhorn , Bernice M. Martin , Carl Franzblau

{"title":"Type IV Collagen Synthesis and Accumulation in Neonatal Rat Aortic Smooth Muscle Cell Cultures","authors":"Ann C. Hospelhorn , Bernice M. Martin , Carl Franzblau","doi":"10.1016/S0934-8832(11)80031-4","DOIUrl":"10.1016/S0934-8832(11)80031-4","url":null,"abstract":"<div><p>The production of type IV collagen by cultured neonatal rat aortic smooth muscle cells was monitored over a three-week period to further characterize the extracellular matrix of this unique culture system. Type IV collagen was quantified using a dot immunobinding assay and was found to represent 1% or less of the total collagen produced by these cells in culture. Total collagen represented up to 33% of the total protein. The pattern of type IV collagen production in the media and the cell layer suggests that although these cells synthesize and secrete type IV collagen from the onset of culture, type IV collagen deposition only occurs after the cells have reached confluence. In the presence of ascorbate the amount of type IV collagen peaked in the media in preconfluent cultuRes In the absence of ascorbate, little type IV collagen was detected in the media. On the other hand, the presence or absence of ascorbate made little difference in the amount of the total collagen detected in the media, although hydroxylation was affected. Remarkably, in the absence of ascorbate type IV collagen accumulation in the cell layer was similar by the end of the culture period to that in cultures treated with ascorbate. Laminin was not affected by the presence or absence of ascorbate. When these cells were exposed to ascorbate for 24 hours, a peak of soluble elastin was detected in the media. However, soluble elastin was not detected in the media in the absence of ascorbate or in cultures which were maintained in the presence of ascorbate. Modulation of the extracellular matrix with ascorbic acid indicated that type IV collagen deposition did not depend on the presence of ascorbic acid and that there was no discernable interaction between type IV collagen, laminin, and elastin.</p></div>","PeriodicalId":77253,"journal":{"name":"Matrix (Stuttgart, Germany)","volume":"12 5","pages":"Pages 352-361"},"PeriodicalIF":0.0,"publicationDate":"1992-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0934-8832(11)80031-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12655010","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 12

An ELISA-like assay for hyaluronidase and hyaluronidase inhibitors 透明质酸酶和透明质酸酶抑制剂的elisa样测定

Matrix (Stuttgart, Germany) Pub Date : 1992-11-01 DOI: 10.1016/S0934-8832(11)80036-3

Michael Stern , Robert Stern

{"title":"An ELISA-like assay for hyaluronidase and hyaluronidase inhibitors","authors":"Michael Stern , Robert Stern","doi":"10.1016/S0934-8832(11)80036-3","DOIUrl":"10.1016/S0934-8832(11)80036-3","url":null,"abstract":"<div><p>Hyaluronic acid (HA) is a prominent molecule in the extracellular matrix and is enriched whenever there is rapid tissue proliferation, regeneration and repair. HA is degraded in part by hyaluronidases (HA'ases) that are not well characterized. We have developed a novel ELISA-like rapid assay for HA'ases and their inhibitors. The assay is based on a high affinity biotinylated HA-binding peptide derived from tryptic digests of proteoglycan core protein of bovine nasal cartilage and the avidin-biotin reaction. HA-coated plates were incubated with serial dilutions of <em>Streptomyces</em> HA'ase, and the undegraded HA was measured. This established a standard curve for HA'ase activity against which all unknown enzyme samples were compared. The assay is easily modified to also serve a measure of HA'ase inhibitors. For detection of inhibitors, aliquots of sample were preincubated with a known activity of HA'ase and inhibition of HA degradation by the mixture was measured. We have used this assay to document the presence of potent HA'ase inhibitors in fetal calf sera. These techniques will aid in the purification and characterization of Ha'ases and their inhibitors.</p></div>","PeriodicalId":77253,"journal":{"name":"Matrix (Stuttgart, Germany)","volume":"12 5","pages":"Pages 397-403"},"PeriodicalIF":0.0,"publicationDate":"1992-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0934-8832(11)80036-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12457894","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 85

Isolation, Characterization and Immunolocalization of a 53-kDal Dentin Sialoprotein (DSP) 53-kDal牙本质唾液蛋白(DSP)的分离、鉴定及免疫定位

Matrix (Stuttgart, Germany) Pub Date : 1992-11-01 DOI: 10.1016/S0934-8832(11)80030-2

William T. Butler , Meera Bhown , Jan C. Brunn , Rena N. D'Souza , Mary C. Farach-Carson , Risto-Pekka Happonen , Ralph E. Schrohenloher , Jerome M. Seyer , Martha J. Somerman , Ruth A. Foster , Milan Tomana , Simon Van Dijk

{"title":"Isolation, Characterization and Immunolocalization of a 53-kDal Dentin Sialoprotein (DSP)","authors":"William T. Butler , Meera Bhown , Jan C. Brunn , Rena N. D'Souza , Mary C. Farach-Carson , Risto-Pekka Happonen , Ralph E. Schrohenloher , Jerome M. Seyer , Martha J. Somerman , Ruth A. Foster , Milan Tomana , Simon Van Dijk","doi":"10.1016/S0934-8832(11)80030-2","DOIUrl":"10.1016/S0934-8832(11)80030-2","url":null,"abstract":"<div><p>We isolated a sialic-rich protein from rat dentin extracts and have named it dentin sialoprotein, DSP (formerly called 95K glycoprotein). DSP is rich in aspartic acid, glutamic acid, glycine and serine, but contains no cysteine or phosphate. The 30% carbohydrate content includes about 9% sialic acid and indicates that several N-glycosides and O-glycosides are present. Sedimentation equilibrium analysis gave a M<sub>r</sub> of 52,570. Based on this molecular weight we calculated that DSP contains about 350-amino acids and 75 monosaccharides. With automated Edman degradation the sequence of the first 8-amino acids was shown to be: Ile-Pro-Val-Pro-Gln-Leu-ValPro. The initial 3 residues of this sequence are identical to the first 3 in human osteopontin (OPN) and are closely similar to the Leu-Pro-Val sequences of OPN from other species, as well as at the beginning of bone acidic glycoprotein-75 (BAG-75).</p><p>On Western immunoblots, purified polyclonal antibodies reacted only with DSP in dentin extracts and with none of the proteins from bone. Similarly, immunolocalization experiments showed the presence of DSP in dentin but not in enamel or alveolar bone. Along with immunohistochemical localization data reported elsewhere, these observations suggest that DSP may be an important marker for cells in the odontoblast lineage.</p></div>","PeriodicalId":77253,"journal":{"name":"Matrix (Stuttgart, Germany)","volume":"12 5","pages":"Pages 343-351"},"PeriodicalIF":0.0,"publicationDate":"1992-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0934-8832(11)80030-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12655009","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 139