{"title":"Chromosomal evolution and speciation in primates.","authors":"Y Rumpler, B Dutrillaux","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"23 ","pages":"1-112"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13255351","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 intracellular proteinases in human neutrophil activation.","authors":"S Pontremoli, E Melloni","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>In addition to other proteinases human neutrophils contain two non granular neutral endopeptidases: a serine proteinase and a cysteine Ca2+ dependent proteinase named calpain. Serine proteinase localized in association with the cytoskeleton-membrane proteins, apparently exerts a dual role: it is partially released into the medium during neutrophil stimulation by phorbol myristate acetate (PMA), presumably acting as one of the cytotoxic factors; and in its intracellular localization is presumably involved in the process of down regulation of native protein kinase C (PKC). Calpain, predominantly present in resting conditions in an inactive form, becomes activated in the course of neutrophil stimulation and appears to be involved both in the down regulation of native PKC as well as in the formation of a proteinase-activated kinase form, presumably derived from PKC and defined as PKC-M. Calpain once activated appears to be also involved in cytoskeleton rearrangement, through proteolytic degradation specifically oriented by substrate phosphorylation. Activation, down regulation of PKC, formation of the proteinase-activated kinase, as well as proteolytic processing of cytoskeleton have been demonstrated to be correlated to those biochemical responses which characterize neutrophil activation.</p>","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"20 ","pages":"161-77"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13704450","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":"Intermediate filaments in biology and disease.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Intermediate filaments comprise a large heterogenous family of proteins in animal cells. Distinct from microfilaments and microtubules, they are a major component of the cytoskeleton and nuclear envelope. The expression of intermediate filament protein types is developmentally regulated and relatively cell type specific. Although there are at least five distinct classes of intermediate filament types, all the subunit proteins have similar structural features and appear to have envolved from some common gene ancestor. The cytoplasmic intermediate filaments exhibit a complex organization, forming associations with components of the nucleus, plasma membrane, and potentially other cytoplasmic structures such as microtubules. The specific function of this prominent cytoplasmic structure is currently unknown. However, the organization or expression of intermediate filaments is known to be altered in association with a variety of human diseases. Currently, specific antibodies to individual intermediate filament proteins are being used as an immunohistochemical aid for tumor typing in diagnostic pathology.</p>","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"22 ","pages":"1-80"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13839221","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":"ATP and 2,3-bisphosphoglycerate: models of metabolites for the regulation of intracellular protein degradation.","authors":"E Roche, F Aniento, E Knecht","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The main question in protein turnover is what determines the susceptibility of a given protein molecule to proteolytic degradation. Much evidence supports a role for the structural characteristics of individual proteins in determining their specific degradation rates. However, changes in the environment can influence these characteristics and thus the degradation rates. Since intracellular proteins in vivo are in a natural environment, substrates, products, cofactors and other low molecular weight compounds are often bound to the proteins, and probably contribute thereby to the vastly different half-lives of proteins. This paper reviews recent results from the authors' laboratory on the possible regulation of intracellular protein degradation by low molecular weight components. We have centered our studies on 2,3-bisphosphoglycerate and ATP, which modify, in opposite directions, the proteolytic susceptibility of specific mitochondrial and cytosolic proteins to lysosomal and non-lysosomal proteases. As shown, these metabolites can also modify the microautophagic uptake of certain proteins as well as the degradation rate of proteins in cultured cells.</p>","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"21 ","pages":"285-304"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13840334","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":"Proteolysis and cell death.","authors":"J S Amenta, F M Baccino","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cell death can occur by a number of different mechanisms, some of which are associated with significant protein degradation. L-cells in monolayer culture were labelled with 14C-leucine and 3H-thymidine and placed in a cold chase medium for each experiment. General cellular necrosis, induced by either repeated freeze-thawing or NaCN, rapidly disrupted cellular structure, but produced only small amounts of acid soluble 14C over a period of 24 h. Selective cell death was produced by adding 5 mM thymidine to growing tissue cultures. With such treatment, cell death became manifest only after a 24 h lag period and progressively more intense in the next 48 h. The process was characterized first by cellular enlargement and protein accumulation, followed by the formation and release of eosinophilic hyaline bodies from cell cytoplasm. These bodies were often found adjacent to the plasma membranes of viable cells, as well as within cellular vacuoles. Biochemical studies indicated that proteolysis was significantly increased; this proteolysis, but not cell death, was prevented by NH4Cl. Cell death, formation of eosinophilic hyaline bodies, and proteolysis were prevented by cycloheximide. Cell cultures that manifest cell turnover, i.e. selective cell death, apoptosis-type, will show increased amounts of vacuolar proteolysis, which may be confused with accelerated protein turnover occurring in the vacuolar system.</p>","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"21 ","pages":"401-22"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13840336","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":"Protease/inhibitor mechanisms involved in ATP-dependent proteolysis.","authors":"J D Etlinger, M Gu, X Li, D Weitman, R F Rieder","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>ATP-dependent proteolytic activities constitute a family of distinct enzymes and enzyme complexes which function in the selective degradation of proteins in the cytosol and possibly other non-lysosomal cellular compartments. In reticulocytes as well as other eukaryotic cells, conjugation of the polypeptide ubiquitin to proteins, an ATP-requiring process, is important for proteolysis. However, the popular view that ubiquitin functions by tagging substrates for recognition by conjugate-specific proteases should be viewed with caution. Evidence is reviewed implicating an ATP-independent high molecular weight protease (HMP) which can degrade non-ubiquitinated proteins in the ATP-dependent pathway. This protease consists of several related subunits based upon monoclonal antibody studies. HMP by itself, can account for effects of substrate amino group blockage on ATP-dependent proteolysis. Endogenous inhibitors (40 kDa and 50 kDa) have been isolated and shown to block HMP non-competitively. Unlike the soluble system in reticulocytes, the major ATP-dependent activity in mouse erythroleukemia cells is particulate in aqueous media but soluble in the presence of sucrose. Despite such differences, evidence suggests analogous inhibitory components in this system. The possibility that protease/inhibitor interaction is regulated by ATP and ubiquitin in different systems is discussed.</p>","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"20 ","pages":"197-216"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13704452","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":"Muscle protein breakdown in premature human infants.","authors":"F J Ballard, R R Haslam, J L Burgoyne, F M Tomas","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Muscle protein breakdown in premature human infants can be quantified from the urinary excretion ratio of 3-methylhistidine (3MH) to creatinine. Only single urine samples are needed and no prior treatment of the infant is required. Use of this procedure over the past 10 years has established that rates of muscle protein breakdown increase rapidly in response to stress, infection or inadequate nutrition and return to normal once successful treatment has been achieved. Higher rates are also observed in very early premature infants. No effects of sex, time of day or the route of nutrient intake, whether parenteral or enteral, are observed. A marked fall in 3MH excretion occurs following indomethacin treatment, consistent with responses to prostaglandin inhibitors established previously in isolated muscle.</p>","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"21 ","pages":"445-57"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13777786","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}
V J Miralles, C González-Bosch, M J Marcote, J Hernández-Yago
{"title":"Selective aspects of mitochondrial protein turnover.","authors":"V J Miralles, C González-Bosch, M J Marcote, J Hernández-Yago","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>To establish the interrelationship between protein synthesis and degradation, we have developed a simple procedure. We have chosen the mitochondrial proteins, because most of them are synthesized outside mitochondria and are then imported into the organelle. This fact allows to separate easily the synthesis steps from the general turnover. By using this system we have some evidences suggesting that the in vitro protein concentration in mitochondria may be regulated by the entry of mitochondrial protein precursors. Also, we are studying the factors that regulate the import of mitochondrial protein precursors into the organelle, because this step may be essential in the regulation of the turnover of mitochondrial proteins.</p>","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"21 ","pages":"461-73"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13704854","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":"Current trends in the study of intracellular protein degradation I.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"20 ","pages":"1-273"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13778217","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":"Proteolytic control over formation of enzymic complexes of the mitochondrial inner membrane.","authors":"V N Luzikov","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Assembly of enzymic complexes of the mitochondrial inner membrane is an intricate process involving import of protein precursors from the cytosol and from the mitochondrial matrix, proteolytic processing of the precursors, covalent and noncovalent attachment of prosthetic groups to apoproteins, diffusion of proteins in the membrane in search of their partners, etc. The aim of the present communication is to draw attention to that, concurrent with all these events, proteolysis of mitochondrial inner membrane proteins occurs, which in some cases is rapid and can play a prominent part in correcting polypeptide compartmentation, subunit stoichiometry in complexes, overall amounts of proteins and mutual arrangement of complexes in the membrane.</p>","PeriodicalId":77783,"journal":{"name":"Revisiones sobre biologia celular : RBC","volume":"21 ","pages":"491-503"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13841942","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}