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Abnormal adherence junctions in the heart and reduced angiogenesis in transgenic mice overexpressing mutant type XIII collagen.

https://arctichealth.org/en/permalink/ahliterature53860
Source
EMBO J. 2001 Sep 17;20(18):5153-64
Publication Type
Article
Date
Sep-17-2001
Author
M. Sund
R. Ylönen
A. Tuomisto
R. Sormunen
J. Tahkola
A P Kvist
S. Kontusaari
H. Autio-Harmainen
T. Pihlajaniemi
Author Affiliation
Collagen Research Unit, Biocenter Oulu, Department of Medical Biochemistry, University of Oulu, PL 5000, 90014 Oulu, Finland.
Source
EMBO J. 2001 Sep 17;20(18):5153-64
Date
Sep-17-2001
Language
English
Publication Type
Article
Keywords
Adherens Junctions - ultrastructure
Animals
Collagen - genetics - metabolism - physiology
Embryonic and Fetal Development
Fetus - abnormalities - blood supply
Heart - embryology
Heart Defects, Congenital - pathology
Mice
Mice, Transgenic
Mutation
Myocardium - ultrastructure
Neovascularization, Physiologic
Phenotype
Placenta - abnormalities - blood supply
RNA, Messenger - biosynthesis
Research Support, Non-U.S. Gov't
Survival Analysis
Abstract
Type XIII collagen is a type II transmembrane protein found at sites of cell adhesion. Transgenic mouse lines were generated by microinjection of a DNA construct directing the synthesis of truncated alpha1(XIII) chains. Shortened alpha 1(XIII) chains were synthesized by fibroblasts from mutant mice, and the lack of intracellular accumulation in immunofluorescent staining of tissues suggested that the mutant molecules were expressed on the cell surface. Transgene expression led to fetal lethality in offspring from heterozygous mating with two distinct phenotypes. The early phenotype fetuses were aborted by day 10.5 of development due to a lack of fusion of the chorionic and allantoic membranes. The late phenotype fetuses were aborted by day 13.5 of development and displayed a weak heartbeat, defects of the adherence junctions in the heart with detachment of myofilaments and abnormal staining for the adherence junction component cadherin. Decreased microvessel formation was observed in certain regions of the fetus and the placenta. These results indicate that type XIII collagen has an important role in certain adhesive interactions that are necessary for normal development.
PubMed ID
11566879 View in PubMed
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Activation and relocalization of caspase 3 during the apoptotic cascade of human mesothelioma cells.

https://arctichealth.org/en/permalink/ahliterature16909
Source
APMIS. 2005 Jun;113(6):426-35
Publication Type
Article
Date
Jun-2005
Author
Y. Soini
K. Kahlos
R. Sormunen
M. Säily
P. Mäntymaa
P. Koistinen
P. Pääkkö
V. Kinnula
Author Affiliation
Department of Pathology, University of Oulu, Finland. msoini@cc.oulu.fi
Source
APMIS. 2005 Jun;113(6):426-35
Date
Jun-2005
Language
English
Publication Type
Article
Keywords
Antibiotics, Antineoplastic - pharmacology
Antigens, CD95 - genetics - metabolism
Apoptosis
Caspases - analysis - metabolism
Enzyme Activation
Epirubicin - pharmacology
Humans
Membrane Glycoproteins - genetics - metabolism
Mesothelioma - enzymology
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured
Abstract
Apoptosis plays an important role in cancer biology. We investigated the expression of caspases 3 and 8 in malignant mesothelioma and malignant mesothelioma cell lines and putative changes in their ultrastructural expression prior and after exposure to epirubicin. Further studies were conducted to compare these changes to the localization and expression of the bcl-2 group of proteins bcl-X, bax and mcl-1, and Fas-Fas ligand in the same cells. In the histological samples, caspase 3 and 8 immunoreactivity was seen in 27/37 (73%) and 16/37 (43%) of the mesotheliomas. The immunostaining was cytoplasmic diffuse, granular, and occasionally nuclear. All six mesothelioma cell lines expressed caspases 3 and 8 by immunoblotting. After exposure to epirubicin the extent of apoptosis was increased in all cell lines investigated, being weakest in the most resistant M38K cell line. Immunoelectron microscopy revealed immunogold labeling for caspases 3 and 8 in the mitochondria with the accumulation of caspase 3 in the apoptotic bodies, while the mitochondrial localization of the bcl-2 proteins appeared to be very stable. Fas receptor could be detected by flow cytometry, whereas the most resistant cell line (M38K) lacked Fas ligand when assessed by RT-PCR. These results suggest the importance of caspase 3 during the apoptotic process of mesothelioma cells and indicate that epirubicin-induced apoptosis is independent of the mitochondrial pathway.
PubMed ID
15996160 View in PubMed
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Apoptosis in operated small cell lung carcinoma is inversely related to tumour necrosis and p53 immunoreactivity.

https://arctichealth.org/en/permalink/ahliterature22201
Source
J Pathol. 1997 Feb;181(2):172-7
Publication Type
Article
Date
Feb-1997
Author
A K Eerola
U. Törmänen
P. Rainio
R. Sormunen
R. Bloigu
K. Vähäkangas
V P Lehto
Y. Soini
P. Pääkkö
Author Affiliation
Department of Pathology, University of Oulu, Finland.
Source
J Pathol. 1997 Feb;181(2):172-7
Date
Feb-1997
Language
English
Publication Type
Article
Keywords
Apoptosis
Carcinoma, Small Cell - metabolism - pathology - surgery
Cell Division
Humans
Immunoenzyme Techniques
Lung Neoplasms - metabolism - pathology - surgery
Necrosis
Neoplasm Proteins - metabolism
Proto-Oncogene Proteins c-bcl-2 - metabolism
Research Support, Non-U.S. Gov't
Tumor Suppressor Protein p53 - metabolism
Abstract
The present study was undertaken to analyse the extent of apoptosis in operated small cell lung carcinoma (SCLC) by using in situ labelling of the oligonucleosomal DNA fragments by terminal transferase. The extent of apoptosis was compared with the cell proliferation activity, as determined by Ki-67 immunohistochemistry; with the volume density of necrosis (per cent), as determined by the morphometric point counting method; and with the occurrence of immunohistochemically detectable p53 and bcl-2 proteins. By in situ labelling, remarkably high apoptotic indices (from 0.08 to 8.10 per cent) were seen in SCLC. A high percentage of SCLSs also showed an exceptionally high proliferation activity. Aberrant accumulation of p53 protein was seen in 37.5 per cent and bel-2 overexpression in 50 per cent of SCLCs. Necrosis was seen in 82.5 per cent of SCLCs. The extent of apoptosis was inversely related to the extent of tumour necrosis (P = 0.05) and to p53 protein accumulation (P = 0.008). A positive association was found between the extent of apoptosis and bel-2 immunoreactivity (P = 0.02). The apoptotic indices (per cent) correlated with the age (P
PubMed ID
9120721 View in PubMed
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Bile canaliculus formation in cultured HEPG2 cells.

https://arctichealth.org/en/permalink/ahliterature24022
Source
Lab Invest. 1993 Jun;68(6):652-62
Publication Type
Article
Date
Jun-1993
Author
R. Sormunen
S. Eskelinen
V P Lehto
Author Affiliation
Biocenter, University of Oulu, Finland.
Source
Lab Invest. 1993 Jun;68(6):652-62
Date
Jun-1993
Language
English
Publication Type
Article
Keywords
Bile Canaliculi - chemistry - growth & development - ultrastructure
Carcinoma, Hepatocellular - chemistry - ultrastructure
Humans
Liver Neoplasms - chemistry - ultrastructure
Microfilament Proteins - analysis
Microscopy, Electron
Microscopy, Immunoelectron
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured
Abstract
BACKGROUND: The plasma membrane of hepatocytes can be divided in sinusoidal, lateral and apical membrane, each with functionally and structurally distinct features. The apical domain consists of the bile canalicular structures. The morphogenesis and the polarization of hepatocytes is still poorly known. EXPERIMENTAL DESIGN: We used HepG2 cells, a hepatoma cell line to study the formation of the bile canaliculi in the apical part of the cells. The cells were synchronized by using nocodazole. The formation of the bile canaliculi was monitored by using immunofluorescence microscopy, confocal laser scanning microscopy, and immunoelectron microscopy. Antibodies to alpha-fodrin and villin were used. Actin was visualized with rhodamine phalloidin. RESULTS: Confocal laser scanning microscopy showed accumulations of actin, villin and fodrin at the cell membranes 8 to 12 hours after the release of the nocodazole block. These sites probably represent areas destined to develop into bile canaliculi. Later, immature bile canaliculi were discerned that were located asymmetrically between adjacent cells. Transmission electron microscopy of serial sections showed that they were always connected with the surface of the cell. Mature bile canaliculi appeared between adjacent cells 48 hours after the release of the nocodazole block. They were round, vesicle-like structures lined with microvilli and sealed by tight junctions and desmosomes. They were usually seen between two juxtaposed cells, and often several cells contributed to their formation. Typically, mature bile canaliculi were delineated by a subplasmalemmal filamentous meshwork of fodrin and actin, resembling a terminal web of enterocytes. Actin and villin were also found in microvillar cores. CONCLUSIONS: The results show that (i) bile canaliculi are formed de novo between two or more juxtaposed cells; (ii) canalicular-formation is accompanied by a distinct accumulation of the membrane skeletal and microvillar proteins fodrin, actin and villin at the apical surfaces of the cells, suggesting that they play an important role in bile canaliculus morphogenesis, and that (iii) apical membrane differentiation in the cells contributing to the formation of a single canaliculus is an asymmetric process.
PubMed ID
8390592 View in PubMed
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Bronchiolo-alveolitis with pulmonary basal lamina injury in a rheumatoid patient during gold treatment.

https://arctichealth.org/en/permalink/ahliterature14557
Source
Pathol Res Pract. 1988 Feb;183(1):46-53
Publication Type
Article
Date
Feb-1988
Author
P. Pääkkö
S. Sutinen
S. Anttila
H. Autio-Harmainen
R. Sormunen
M. Hakala
J. Jouppila
Author Affiliation
Department of Pathology, University of Oulu, Finland.
Source
Pathol Res Pract. 1988 Feb;183(1):46-53
Date
Feb-1988
Language
English
Publication Type
Article
Keywords
Alveolitis, Extrinsic Allergic - chemically induced - pathology
Arthritis - drug therapy
Basement Membrane - ultrastructure
Bronchiolitis - chemically induced - pathology
Female
Gold Sodium Thiomalate - adverse effects
Humans
Immunohistochemistry
Lung - ultrastructure
Microscopy, Electron
Middle Aged
Pulmonary Alveoli
Research Support, Non-U.S. Gov't
Abstract
A 47-year-old housewife presented with nonproductive cough, progressive breathlessness and intermittent fever during gold treatment, originally prescribed for seropositive polyarthritis, which later fulfilled the criteria for systemic lupus erythematosus (SLE). An open lung biopsy showed abundant interstitial edema with mononuclear inflammatory cells and some eosinophils, and slight bronchiolitis. The picture was nonspecific but suggestive of hypersensitivity pneumonitis. Electron microscopy revealed splitting and local disappearance of the basal laminae of the alveolar capillaries, venules and alveolar epithelium. This injury was confirmed by immunohistochemical staining for type IV collagen and laminin, the major components of basal laminae. In most macrophages there was lysosomal electron dense granular material, i.e. aurosomes, which gave the spectrum of gold in electron microprobe analysis. After the gold treatment was stopped the pulmonary symptoms gradually decreased during several months and no permanent lung disease remained. Whereas the pulmonary manifestation could have been due to her underlying disease we discuss in this study the possibility of its being gold induced.
PubMed ID
3129704 View in PubMed
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Enhanced apoptosis predicts shortened survival in non-small cell lung carcinoma.

https://arctichealth.org/en/permalink/ahliterature22996
Source
Cancer Res. 1995 Dec 1;55(23):5595-602
Publication Type
Article
Date
Dec-1-1995
Author
U. Törmänen
A K Eerola
P. Rainio
K. Vähäkangas
Y. Soini
R. Sormunen
R. Bloigu
V P Lehto
P. Pääkkö
Author Affiliation
Department of Pathology, University of Oulu, Finland.
Source
Cancer Res. 1995 Dec 1;55(23):5595-602
Date
Dec-1-1995
Language
English
Publication Type
Article
Keywords
Aged
Aged, 80 and over
Apoptosis - physiology
Carcinoma, Non-Small-Cell Lung - chemistry - mortality - pathology
Female
Humans
Lung Neoplasms - chemistry - mortality - pathology
Male
Middle Aged
Prognosis
Proliferating Cell Nuclear Antigen - analysis
Proto-Oncogene Proteins - analysis
Proto-Oncogene Proteins c-bcl-2
Research Support, Non-U.S. Gov't
Tumor Markers, Biological - analysis
Tumor Suppressor Protein p53 - analysis
Abstract
This study was undertaken to determine the extent of apoptosis in lung carcinoma and to evaluate it as a prognostic marker. A series of 75 lung carcinomas (47 squamous cell carcinomas, 24 adenocarcinomas, 3 small cell carcinomas, and 1 large cell carcinoma) was analyzed for the extent of apoptosis by using the 3' end-labeling method of DNA in tissue sections. Apoptosis was correlated with the rate of cell proliferation, the immunohistochemically detectable p53 and bcl-2, the extent of tumor necrosis, and the survival data. The end-labeling method allowed a precise evaluation of the extent of apoptosis. In tumor tissue, the number of apoptotic bodies was roughly 2-fold greater than the number of apoptotic cells, whereas in nonneoplastic control tissues, the ratio was 1:1. The apoptotic indexes (percentages of apoptotic cells and bodies among tumor cells) were slightly higher in adenocarcinoma than in squamous cell carcinoma. There was no association between the extent of apoptosis and the expression of proliferating cell nuclear antigen or p53. On the other hand, tumor necrosis correlated significantly with proliferating cell nuclear antigen and p53 positivity (P = 0.00025 and 0.00087, respectively). Surprisingly, the extent of apoptosis was also found to be independent of the expression of bcl-2. Patients with apoptotic indexes greater than 1.5% had significantly shorter survival time than patients with apoptotic indexes equal to 1.50% or less (P
PubMed ID
7585640 View in PubMed
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Expression and prognostic significance of catalase in malignant mesothelioma.

https://arctichealth.org/en/permalink/ahliterature19913
Source
Cancer. 2001 Apr 1;91(7):1349-57
Publication Type
Article
Date
Apr-1-2001
Author
K. Kahlos
Y. Soini
R. Sormunen
R. Kaarteenaho-Wiik
P. Pääkkö
K. Linnainmaa
V L Kinnula
Author Affiliation
Department of Internal Medicine, University of Oulu, FIN-90220, Oulu, Finland.
Source
Cancer. 2001 Apr 1;91(7):1349-57
Date
Apr-1-2001
Language
English
Publication Type
Article
Keywords
Amitrole - pharmacology
Blotting, Western
Catalase - metabolism
Epirubicin - pharmacology
Humans
Immunohistochemistry
Mesothelioma - enzymology - mortality
Microscopy, Immunoelectron
Pleural Neoplasms - enzymology - mortality
Prognosis
Research Support, Non-U.S. Gov't
Superoxide Dismutase - metabolism
Survival Rate
Tumor Cells, Cultured
Tumor Markers, Biological - analysis
Abstract
BACKGROUND: Free radicals and antioxidant enzymes (AOEs) may play a critical role in cell proliferation and in the resistance of malignant cells against cytotoxic drugs and radiation. Malignant mesothelioma is a resistant tumor with high levels of manganese superoxide dismutase, a central superoxide scavenging AOE. In the current study, the authors assessed the expression and prognostic role of catalase, an important hydrogen peroxide scavenging AOE, in malignant pleural mesothelioma. METHODS: Catalase expression was investigated by immunohistochemistry in 5 cases of nonmalignant healthy pleura and in tumor tissue of 32 mesothelioma patients, and by Western blot in 7 continuous human mesothelioma cell lines. The distribution of catalase in mesothelioma cells was assessed by immunoelectron microscopy. Furthermore, to investigate the effect of catalase inhibition in the drug resistance of these cells in vitro, the authors exposed mesothelioma cells with the highest catalase level to epirubicin with and without aminotriazole pretreatment. RESULTS: Nonmalignant mesothelial cells showed no catalase immunoreactivity whereas most mesothelioma cases (24 of 32, 75%) were catalase positive, 17 cases (53%) showing moderate or high expression. Higher catalase expression in mesothelioma was associated with a better prognosis, mean survival rate from diagnosis being 6 and 24 months for negative/low expression and moderate/high expression, respectively. Furthermore, a coordinately high expression of both manganese-superoxide dismutase (Mn-SOD) and catalase predicted even more favorable outcome of the mesothelioma patients. Catalase also could be detected in all mesothelioma cell lines, the most resistant cell line showing the highest protein expression and compartmentalization of catalase mainly to peroxisomes. Aminotriazole inhibition of catalase had a marginal effect on the toxicity caused by epirubicin. CONCLUSIONS: Catalase may have multifactorial effects in malignant cells; high catalase and/or coordinated high expression of Mn-SOD and catalase may decrease tumor progression by modulating the cellular redox state, but enhanced antioxidant capacity of mesothelioma cells also may protect tumor cells against exogenous oxidants, at least in vitro.
PubMed ID
11283936 View in PubMed
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Fodrin and actin in the normal, metaplastic, and dysplastic respiratory epithelium and in lung carcinoma.

https://arctichealth.org/en/permalink/ahliterature23608
Source
Am J Respir Cell Mol Biol. 1994 Jul;11(1):75-84
Publication Type
Article
Date
Jul-1994
Author
R. Sormunen
P. Pääkkö
R. Palovuori
Y. Soini
V P Lehto
Author Affiliation
Biocenter, University of Oulu, Finland.
Source
Am J Respir Cell Mol Biol. 1994 Jul;11(1):75-84
Date
Jul-1994
Language
English
Publication Type
Article
Keywords
Actins - analysis
Animals
Antibodies, Monoclonal
Bronchi - chemistry
Carrier Proteins - analysis
Chickens
Epithelium - chemistry - pathology
Fluorescent Antibody Technique
Humans
Immunoblotting
Lung Neoplasms - chemistry - pathology
Microfilament Proteins - analysis
Microscopy, Fluorescence
Microscopy, Immunoelectron
Pulmonary Alveoli - chemistry
Research Support, Non-U.S. Gov't
Tissue Distribution
Abstract
Distribution of actin and fodrin, a nonerythroid analogue of spectrin, was studied in cytocentrifuge preparations and in tissue sections of normal and pathologic respiratory epithelium by using immunofluorescence and immunoelectron microscopy. In ciliated epithelial cells and in goblet cells of normal bronchial epithelium, fodrin and actin were located in the apical parts and along the lateral walls of the cells. In basal cells, fodrin and actin were also seen diffusely in the cytoplasm. Immunoelectron microscopy showed fodrin in close association with the basal bodies and rootlets of the cilia and microvilli in the ciliated cells. In alveolar epithelium, fodrin and actin were located at the apical membrane in type I pneumocytes and along the apical and lateral membranes in type II pneumocytes. In type II pneumocytes, fodrin was also seen in close association with the secretory vacuoles. In metaplastic and dysplastic bronchial epithelium, a diffuse cytoplasmic and a circumferential, membrane-associated staining for fodrin and actin was seen. In all types of carcinomas, fodrin was seen along the lateral walls and diffusely in the cytoplasm. The staining was more intense than in the normal cells. In immunoblotting of the normal bronchial epithelium, and peripheral lung and lung carcinomas, a single 240 kD band was recognized with antibodies to fodrin. The results show distinct differences in the distribution of fodrin in the various cell types of the respiratory epithelium. In ciliated cells, the close relationship with cytoskeleton suggests a role of fodrin in the establishment of the elaborate structural architecture of the apical compartment. In type II pneumocytes, on the other hand, fodrin probably plays a role in secretion of the surfactant. In basal cells, the diffuse distribution of fodrin probably reflects the high proliferative capacity of this cell compartment. Interestingly, a similar distribution was also seen in premalignant and malignant cells.
PubMed ID
8018340 View in PubMed
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Lack of cytosolic and transmembrane domains of type XIII collagen results in progressive myopathy.

https://arctichealth.org/en/permalink/ahliterature49856
Source
Am J Pathol. 2001 Oct;159(4):1581-92
Publication Type
Article
Date
Oct-2001
Author
A P Kvist
A. Latvanlehto
M. Sund
L. Eklund
T. Väisänen
P. Hägg
R. Sormunen
J. Komulainen
R. Fässler
T. Pihlajaniemi
Author Affiliation
Department of Medical Biochemistry, Biocenter Oulu, University of Oulu, Oulu, Finland.
Source
Am J Pathol. 2001 Oct;159(4):1581-92
Date
Oct-2001
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence - genetics
Animals
Cell Adhesion - physiology
Cell Membrane - metabolism
Cells, Cultured
Collagen Type XIII - chemistry - genetics - metabolism
Cytosol - metabolism
Disease Progression
Exons
Fibroblasts - physiology
Gene Deletion
Mice
Mice, Transgenic
Microscopy, Immunoelectron
Molecular Sequence Data
Motor Activity
Muscle, Skeletal - pathology - ultrastructure
Muscular Diseases - etiology - pathology - physiopathology
Protein Structure, Tertiary
Recombination, Genetic
Research Support, Non-U.S. Gov't
Abstract
Type XIII collagen is a type II transmembrane protein found at many sites of cell adhesion in tissues. Homologous recombination was used to generate a transgenic mouse line (Col13a1(N/N)) that expresses N-terminally altered type XIII collagen molecules lacking the short cytosolic and transmembrane domains but retaining the large collagenous ectodomain. The mutant molecules were correctly transported to focal adhesions in cultured fibroblasts derived from the Col13a1(N/N) mice, but the cells showed decreased adhesion when plated on type IV collagen. These mice were viable and fertile, and in immunofluorescence stainings the mutant protein was located in adhesive tissue structures in the same manner as normal alpha1(XIII) chains. In immunoelectron microscopy of wild-type mice type XIII collagen was detected at the plasma membrane of skeletal muscle cells whereas in the mutant mice the protein was located in the adjacent extracellular matrix. Affected skeletal muscles showed abnormal myofibers with a fuzzy plasma membrane-basement membrane interphase along the muscle fiber and at the myotendinous junctions, disorganized myofilaments, and streaming of z-disks. The findings were progressive and the phenotype was aggravated by exercise. Thus type XIII collagen seems to participate in the linkage between muscle fiber and basement membrane, a function impaired by lack of the cytosolic and transmembrane domains.
PubMed ID
11583983 View in PubMed
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Lack of type XV collagen causes a skeletal myopathy and cardiovascular defects in mice.

https://arctichealth.org/en/permalink/ahliterature49901
Source
Proc Natl Acad Sci U S A. 2001 Jan 30;98(3):1194-9
Publication Type
Article
Date
Jan-30-2001
Author
L. Eklund
J. Piuhola
J. Komulainen
R. Sormunen
C. Ongvarrasopone
R. Fássler
A. Muona
M. Ilves
H. Ruskoaho
T E Takala
T. Pihlajaniemi
Author Affiliation
Collagen Research Unit, Biocenter Oulu and Departments of Medical Biochemistry, Pharmacology and Toxicology, Pathology, and Physiology, University of Oulu, 90014 Oulu, Finland.
Source
Proc Natl Acad Sci U S A. 2001 Jan 30;98(3):1194-9
Date
Jan-30-2001
Language
English
Publication Type
Article
Keywords
Animals
Apoptosis
Capillaries - pathology - physiopathology - ultrastructure
Cardiovascular Diseases - genetics - pathology - physiopathology
Collagen - deficiency - genetics - physiology
Enzyme Precursors - analysis
Gelatinases - analysis
Glucuronidase - analysis
Heart - physiology - physiopathology
In Vitro
Metalloendopeptidases - analysis
Mice
Mice, Knockout
Muscle Fibers - pathology
Muscle, Skeletal - pathology
Muscular Diseases - genetics - pathology - physiopathology
Myocardium - pathology
Regeneration
Research Support, Non-U.S. Gov't
Abstract
Type XV collagen occurs widely in the basement membrane zones of tissues, but its function is unknown. To understand the biological role of this protein, a null mutation in the Col15a1 gene was introduced into the germ line of mice. Despite the complete lack of type XV collagen, the mutant mice developed and reproduced normally, and they were indistinguishable from their wild-type littermates. However, Col15a1-deficient mice showed progressive histological changes characteristic for muscular diseases after 3 months of age, and they were more vulnerable than controls to exercise-induced muscle injury. Despite the antiangiogenic role of type XV collagen-derived endostatin, the development of the vasculature appeared normal in the null mice. Nevertheless, ultrastructural analyses revealed collapsed capillaries and endothelial cell degeneration in the heart and skeletal muscle. Furthermore, perfused hearts showed a diminished inotropic response, and exercise resulted in cardiac injury, changes that mimic early or mild heart disease. Thus, type XV collagen appears to function as a structural component needed to stabilize skeletal muscle cells and microvessels.
PubMed ID
11158616 View in PubMed
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