Y Kapanci, P M Costabella, P Cerutti, A Assimacopoulos
{"title":"Distribution and function of cytoskeletal proteins in lung cells with particular reference to 'contractile interstitial cells'.","authors":"Y Kapanci, P M Costabella, P Cerutti, A Assimacopoulos","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cytoskeletal proteins are demonstrated in the interstitial cells of the lungs. These proteins appear in the cytoplasm as bundles of microfilaments, the individual filaments measuring 40--80 A in diameter. The presence of actin and myosin in these cells is demonstrated by immunofluorescence. Antiactin antibodies (AAA) obtained from patients with chronic aggressive hepatitis, as well as AAA and antimyosin antibodies prepared in the rabbit, are used. The major difference between the cytoskeletal proteins of interstitial cells and other cells of the alveolar tissue (type II epithelium, pericytes, and near the junctional complexes of endothelial cells) is that the microfilaments within the interstitial cells are organized into bundles forming tiny intracytoplasmic 'muscles'. Furthermore, they appear to be much more abundant and seem to anchor the cell on the alveolar basement membrane by hemidesmosome-like structures. These peculiar cytological features provide these cells with an important functional capacity. Being located in the 'pillars' which cross the capillary space, the contraction of interstitial cells may modify the alveolocapillary configuration in some circumstances. The physiological importance of such an 'active' alveolar motility is to provide the lung with a mechanism of autoregulation of the ventilation/perfusion (V/Q) ratio at alveolar level.</p>","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"9 ","pages":"147-68"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11577971","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}
{"title":"The contractile system of blood platelets and its function.","authors":"I Cohen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The various manifestations of platelet activation are derived from a reorganization of components of the contractile and microtubular systems. The controversial initial stages of excitation-contraction coupling in platelets lead to the release of calcium from the dense tubular system, the morphological counterpart of the muscle sarcotubular closed vesicles. Calcium triggers the actin-myosin interaction and the developing force, possibly together with a local increase of the cation concentration, may cause the collapse of the microtubular ring and its reappearance in the forming long pseudopodia. Actin-myosin interaction is modulated by several factors among which tropomyosin-troponin, responsible for the calcium-sensitivity of contractile processes, and phosphorylation of one of the myosin light chains. Platelet actin is anchored to the membrane and its sliding towards the short myosin filaments may form the basis for platelet shape change. Platelet alpha-actinin and actin-binding protein are able to aggregate actin into an impressive gel. Therefore, the contractile proteins seem to have a double role in controlling the consistency of the cytoplasmic gel on the one hand, and the contractile manifestations related to motility on the other hand. One of the most important features of the 'contracted' platelet is the rigidity of the pseudopodia brought about by the 'gelification' of actin filaments and the presence of microtubules. A new model for clot contraction is proposed, based on the rigidity of the long spiky pseudopodia and on the motile properties of platelets. While migrating towards each other, the interlocking pseudopodia from different platelets adhere to the polymerizing fibrin, compressing the fibrin nets in their pathway. Since the anchoring of contractile fibers to membranes is crucial for the platelet contractile manifestations, the integrity of the membrane structure should be considered in the study of pathological aspects of platelet function.</p>","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"9 ","pages":"40-86"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11577975","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}
{"title":"Interaction of microtubules and microfilaments in platelet contractile physiology.","authors":"J G White, J M Gerrard","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"9 ","pages":"1-39"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11432054","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}
{"title":"The role of the cytoskeleton in pancreatic B-cell function.","authors":"W J Malaisse, L Orci","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The ultrastructural organization of B-cell microtubular-microfilamentous system, its alteration by several pharmacological agents and the concomitant changes in the dynamics of insulin release, the biochemical characterization of islet tubulin and actin, the involvement of microtubules in the process of proinsulin biosynthesis and conversion, the analysis of motile events in endocrine pancreatic cells, the possible participation of microtubular-microfilamentous structures in cell surface organization of the B-cell, and the anomaly of the microtubular apparatus in certain pathological conditions are reviewed. The experimental data support the view that microtubules and microfilaments play an essential role in the process of insulin synthesis and release, as well as in the mechanism of glucagon secretion.</p>","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"9 ","pages":"112-36"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11577969","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}
{"title":"The role of cytoskeleton in neuron activity.","authors":"S Puszkin, W Schook","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The extensive cytoskeleton present in brain tissue is composed of microfilaments, neurofilaments, and neurotubules. A clear understanding of each of these structures is required to accurately define their participation in neuronal functions. Until more is known, therefore, we are restricted to speculate on their importance to the general activity of the cell. The presence of microfilamentous proteins in nerve endings -- the sites where nerve transmission is chemically sustained -- strongly suggests their participation in the release of putative neurotransmitters, a hypothesis that may be substantiated in the near future. It follows that alteration in assembly, disassembly, or interaction among the various cytoskeletal components may permit some insight into the causes and origins of a variety of neurological alterations affecting humankind.</p>","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"9 ","pages":"87-111"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11305185","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}
{"title":"The cytoskeleton in cancer cells in animals and humans.","authors":"G Gabbiani","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Immunofluorescent staining of human cancer cells with antibodies against actin and myosin shows an important increase of brightness when compared with staining of normal cells from control tissues. Electron microscopic examination of cancer cells shows accumulation of cytoplasmic microfilaments (40--80 A in diameter) with some larger filaments (100--120 A in diameter) scattered in between compared to normal cells from control tissues. Such filaments are particularly abundant at the cell periphery. These findings indicate that the cytoplasmic contractile apparatus of cancer cells is more developed than that of normal cells. Such development may at least in part explain the invasive activity of malignant cells.</p>","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"9 ","pages":"231-43"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11577973","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}
{"title":"Leucocytic movement and contractile protein.","authors":"N Senda, N Shibata, H Tamura, J Yoshitake","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>In a study on leucocytic movement, it was found that leucocytes showed periodical dynamic patterns with each motile function, and a possible organization in their motile system. It was also clarified that the motile form and function of leucocytes were co-ordinately controlled by the intracellular level of ATP and that the characteristic contraction wave observed in moving leucocytes was substantial as a morphological manifestation of the contractile element in moving leucocytes. Based on these findings, an attempt was made to extract contractile protein from leucocytes. It was shown that the protein consisted mainly of myosin and actin, which is similar to protein of muscle. Thus, it was concluded that development of the pseudopod, which is indispensable for cell movement, seemed to result from liquid substance in the granuloplasm being squeezed out through contraction of contractile protein located in the surface layer of the granuloplasm. In non-muscular cells, the same type of ordered structure as seen in muscle has not been found yet, but it seems likely that the protein is capable of converting chemical energy into movement.</p>","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"9 ","pages":"169-86"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11962619","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}
{"title":"The cytoskeleton in cultured cells: coordinate in vitro regulation of cell growth and shape.","authors":"R E Pollack, L Kopelovich","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Adenopolyposis of the colon and rectum (ACR) links the well-characterized phenomena of murine oncogenic virus transformation with the progression of a human cancer. The same syndrome links defects in fibroblast growth control and cytoskeletal organization to a tumor of epithelial origin. Since skin fibroblasts are involved in this colonic tumor, the syndrome is very likely to be systemic. That is, one element of normal growth regulation of epithelial cells in situ may be provided by the fibroblasts residing beneath their basement membrane. These observations have led to a novel approach to early detection of persons at risk for a tumor, via the behavior of their skin fibroblasts in culture. At present, it is rarely possible to detect persons at risk for malignancy before the appearance of a frank invasive or metastatic growth. Although many biochemical assays have been proposed as indicators of pre-malignant states or cryptic early tumors, most have eventually been shown to be related to age, sex drug treatment, or other variables linked to but not clearly indicative of, a malignancy. Two serious problems limiting attempts to detect preneoplastic states or a disposition to eventual neoplasia are the inherent low frequency of incidence of any single type of tumor and the difficulty of obtaining identical sample material from prospective or actual patients once they are located. Our approach to these problems significantly departs from the common dependence upon isolation of cells from the site of a tumor. Clearly, it is an easier task to scan skin fibroblasts for disrupted cytoskeletal patterns than it is to obtain epithelia cells from most tissues at high risk for malignancy. This line of work, buttressed by information derived from the model system of SV40 transformation, may provide a novel mode of early detection of other human malignancies, as it has for ACR.</p>","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"9 ","pages":"207-30"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11577972","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}
{"title":"The cytoskeleton and plasma membrane.","authors":"R R Weihing","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The major cytoskeletal elements (microfilaments, microtubules, and 10-nm filaments) are frequently found attached to or near the plasma membrane in arrays which can sometimes be shown experimentally to be related to cell form and movement. Ultrastructural investigations show that attachment is direct, by amorphous electron-dense material, by cell-cell junctions, or by cell-substrate attachment sites, but the chemistry of attachment is poorly understood. The structural and functional polarity of the attached elements has been defined for some microfilaments attached to plasma membrane, but this important parameter has been investigated only slightly for microtubules and not at all for 10-nm filaments attached to membranes. Assemblies of cytoskeletal elements and plasma membrane evidently are structurally stable enough to be observable by electron microscopy and to survive isolation by the usual biochemical techniques, but observations of living cells show that many assemblies of cytoskeleton and plasma membrane undergo rearrangement and interconversion. The biochemical basis and physiological meaning of many of these changes are poorly understood.</p>","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"8 ","pages":"42-109"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11578057","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}
{"title":"The role of cytoskeleton in adreno-medullary secretion.","authors":"P H Cooke, A M Poisner","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Chromaffin cells of the adrenal medulla contain prominent arrays of microtubules and microfilaments. One population of microtubules radiates from the cytocentrum and permeates the areas of the cytoplasm containing chromaffin granules; the other population of microtubules forms a subplasmalemmal network together with actin-like microfilaments. Hence, the cytoskeletal elements in chromaffin cells are strategically located to participate in the mobility of chromaffin granules to the cell surface and to regulate access of the granules to the plasma membrane during exocytosis. Agents which effect the integrity of the cytoskeleton clearly affect the secretory process in a manner which indicates that the microtubules and microfilaments play an active role in the release process.</p>","PeriodicalId":76154,"journal":{"name":"Methods and achievements in experimental pathology","volume":"9 ","pages":"137-46"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11577970","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}