The unlabelled peroxidase-antiperoxidase (PAP) method was applied to the nervous tissue, to investigate whether there are cells which show the localisation of immunoglobulins of IgG, IgA and IgM type. The experiments performed have shown no positive reaction with the PAP method in normal brain tissue. In tumor tissue some cells, rich in cytoplasm of gemistocyte-like appearance or reactive astrocytes stained positively with the PAP method. The reliablility and specificity of the reaction is discussed.
{"title":"On the application of the unlabelled peroxidase-antiperoxidase method to the investigations of the nervous tissue.","authors":"J Kałuza, J Stachura","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The unlabelled peroxidase-antiperoxidase (PAP) method was applied to the nervous tissue, to investigate whether there are cells which show the localisation of immunoglobulins of IgG, IgA and IgM type. The experiments performed have shown no positive reaction with the PAP method in normal brain tissue. In tumor tissue some cells, rich in cytoplasm of gemistocyte-like appearance or reactive astrocytes stained positively with the PAP method. The reliablility and specificity of the reaction is discussed.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"21 1","pages":"67-73"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17256401","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}
A histochemical study has been carried out on the eye muscles of the carp. On the base of the ATP-ase and SDH activity and with regard to the localization and diameter of muscle fibres six types of muscle fibres situated in the defined zones can be distinguished. The type 1 and 2 fibres display a moderately high ATP-ase activity at pH 9.4 and rather low activity after alkaline and acid preincubation. Type 1 shows a high SDH activity in contrast to type 2 with a low SDH activity. The other four types of fibres have the high ATP-ase activity at pH 9.4. Type 3 contains fibres with a moderately high ATP-ase activity after alkaline preincubation with a rather low activity after acid preincubation and with a low SDH activity. The fibres of type 4 characterized by the high ATP-ase activity after alkaline and acid preincubation and by the high SDH activity. The fibres of type 5 display high ATP-ase activity after alkaline and acid preincubation and the low SDH activity. They are situated in the white and intermediate fibre zones. The fibres of type 6 are comparable to the fibres of type 5, however they differ diameter and localization, i.e. they are situated in small diameter fibre zone. Using the electron microscope four types of fibres (A, B, C, and D) are found. They vary in the localization of T system, the organization of Z-line and in M-line appearance. In the type B of muscle fibres two different localizations of T system have been discerned.
{"title":"Muscle fibre composition of the eye muscles of the carp (Cyprinus carpio L.) defined on the base of histochemical observations.","authors":"B Zawadowska, W Kilarski","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A histochemical study has been carried out on the eye muscles of the carp. On the base of the ATP-ase and SDH activity and with regard to the localization and diameter of muscle fibres six types of muscle fibres situated in the defined zones can be distinguished. The type 1 and 2 fibres display a moderately high ATP-ase activity at pH 9.4 and rather low activity after alkaline and acid preincubation. Type 1 shows a high SDH activity in contrast to type 2 with a low SDH activity. The other four types of fibres have the high ATP-ase activity at pH 9.4. Type 3 contains fibres with a moderately high ATP-ase activity after alkaline preincubation with a rather low activity after acid preincubation and with a low SDH activity. The fibres of type 4 characterized by the high ATP-ase activity after alkaline and acid preincubation and by the high SDH activity. The fibres of type 5 display high ATP-ase activity after alkaline and acid preincubation and the low SDH activity. They are situated in the white and intermediate fibre zones. The fibres of type 6 are comparable to the fibres of type 5, however they differ diameter and localization, i.e. they are situated in small diameter fibre zone. Using the electron microscope four types of fibres (A, B, C, and D) are found. They vary in the localization of T system, the organization of Z-line and in M-line appearance. In the type B of muscle fibres two different localizations of T system have been discerned.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"21 2","pages":"115-26"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17288904","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}
The histochemistry of the clitellar glands of Tubiflex tubiflex is reported, together with the ultrastructure of mature secretion units. The distribution and ultrastructure of mucous and granule cells are consistent with published accounts of tubificid citella, thus indicating an absence of intrageneric variation. Mucous cells contain homogenous electron lucent globules which are rich in neutral and acidic mucopolysaccharides and are non-reactive with techniques designed to reveal protein. Type I cells possess structured granules composed of tyrosine-containing basic protein and carboxylated acid mucopolysaccharides. The granules of type II cells are heterogenous and contain several 0.3--0.7 micrometer inclusions of acidic protein with identifiable tyrosine, tryptophan and cystine. The inclusions occur within a matrix composed of neutral mucopolysaccharides and carboxymucin. Type III cell granules possess 0.2--0.5 micrometer inclusions within an electron dense matrix and are rich in neutral and carboxylated acid mucopolysaccharides and basic protein containing tyrosine, tryptophane and cystine. Clitelar carboxymucins are characterized by their stability to beta-glucoronidase, hyaluronidase, neurominidase and acid hydrolysis. A pyridine-extractable lipid moiety within the clitellar secretions was not detected. The results are discussed in relation to cell function during cocoon deposition and, comparatively, with those documented for other oligochaete families.
{"title":"The histochemistry of the clitellum of Tubifex tubifex (annelida: oligochaeta).","authors":"T P Fleming, P J Baron","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The histochemistry of the clitellar glands of Tubiflex tubiflex is reported, together with the ultrastructure of mature secretion units. The distribution and ultrastructure of mucous and granule cells are consistent with published accounts of tubificid citella, thus indicating an absence of intrageneric variation. Mucous cells contain homogenous electron lucent globules which are rich in neutral and acidic mucopolysaccharides and are non-reactive with techniques designed to reveal protein. Type I cells possess structured granules composed of tyrosine-containing basic protein and carboxylated acid mucopolysaccharides. The granules of type II cells are heterogenous and contain several 0.3--0.7 micrometer inclusions of acidic protein with identifiable tyrosine, tryptophan and cystine. The inclusions occur within a matrix composed of neutral mucopolysaccharides and carboxymucin. Type III cell granules possess 0.2--0.5 micrometer inclusions within an electron dense matrix and are rich in neutral and carboxylated acid mucopolysaccharides and basic protein containing tyrosine, tryptophane and cystine. Clitelar carboxymucins are characterized by their stability to beta-glucoronidase, hyaluronidase, neurominidase and acid hydrolysis. A pyridine-extractable lipid moiety within the clitellar secretions was not detected. The results are discussed in relation to cell function during cocoon deposition and, comparatively, with those documented for other oligochaete families.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"20 3-4","pages":"109-27"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17251415","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}
In antheridial filaments of Chara vulgaris L. (cell cycle S+G2+M type) cycloheximide (2.5 micrograms/ml) totally inhibits protein synthesis after 2 h. The protein synthesis is resumed after the removal of the inhibitor from the medium. The inhibition of protein synthesis in the second half of G2 phase causes supercontraction of mitotic chromosomes, whereas in the late G2 phase it induces diminishing of tubulin content and the inhibition of the initiation of DNA synthesis in the next generation of antheridial filaments. The inhibition of protein synthesis in G2 phase does not affect the mitotic index. The inhibition of protein synthesis during S phase results in a lower rate of DNA replication and the prolongation of S phase. The inhibition of protein synthesis in the second half of G2 phase of the previous generation and in the S phase of the given generation causes mitotic delay which increases in proportion to the duration of G2 phase in the given generation.
{"title":"Cell cycle control in synchronously dividing antheridial filaments of Chara vulgaris L. as revealed by cycloheximide pulse treatment.","authors":"M J Olszewska, A Bilecka, H Kuran, K Marciniak","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>In antheridial filaments of Chara vulgaris L. (cell cycle S+G2+M type) cycloheximide (2.5 micrograms/ml) totally inhibits protein synthesis after 2 h. The protein synthesis is resumed after the removal of the inhibitor from the medium. The inhibition of protein synthesis in the second half of G2 phase causes supercontraction of mitotic chromosomes, whereas in the late G2 phase it induces diminishing of tubulin content and the inhibition of the initiation of DNA synthesis in the next generation of antheridial filaments. The inhibition of protein synthesis in G2 phase does not affect the mitotic index. The inhibition of protein synthesis during S phase results in a lower rate of DNA replication and the prolongation of S phase. The inhibition of protein synthesis in the second half of G2 phase of the previous generation and in the S phase of the given generation causes mitotic delay which increases in proportion to the duration of G2 phase in the given generation.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"20 1-2","pages":"3-24"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18155001","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}
Qualitative histochemical studies were carried out on lateral musculature of Carassius auratus gibelio. On the basis of some metabolic enzymes (SDH, LDH) and myofibrillar ATP-ase activities, red, intermediate, white and small diameter muscle fibers were discerned. When SDH method was used, two other fiber types were distinguished. They built up a transition zone, which lay between intermediate and white muscle fiber complexes. The histochemical reaction for myofibrillar ATP-ase activity, after alkaline preincubation, revealed so called "displaced fibers" located at periphery of red as well as intermediate zones.
{"title":"Histochemical analysis of muscle fibers in myotome of teleost fishes (Carassius auratus gibelio).","authors":"L Tatarczuch, W Kilarski","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Qualitative histochemical studies were carried out on lateral musculature of Carassius auratus gibelio. On the basis of some metabolic enzymes (SDH, LDH) and myofibrillar ATP-ase activities, red, intermediate, white and small diameter muscle fibers were discerned. When SDH method was used, two other fiber types were distinguished. They built up a transition zone, which lay between intermediate and white muscle fiber complexes. The histochemical reaction for myofibrillar ATP-ase activity, after alkaline preincubation, revealed so called \"displaced fibers\" located at periphery of red as well as intermediate zones.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"20 3-4","pages":"163-70"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17282446","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}
Cells of antheridial filaments in Chara vulgaris L. blocked at the early G2 phase by a 5 day dark treatment were studied cytologically in order to determine causes of their heterogeneous response to light-induced mitotic activation. Cell size distribution patterns in dark inhibited populations were shown to be nearly consistent with those found within the control populations, comprising all the stages of interphase; cells which resume divisions in response to photoinduction attain, however, sizes characteristic of mitosis occurring in natural light conditions. Cytophotometric determinations of nuclei in cells given dark treatment indicated a complete homogeneity of populations in respect of replicated DNA contents. As evidence by nucleus-cytoplasm surface relations, interferometric measurements of their dry mass contents, and EM stereometric studies, the heterogeneity of early G2 phase arrested populations results from an imbalance between nuclear DNA-division cycle, which is continued up to the early stage of the G2 period, and the growth cycle, which in turn, due to its pronounced inhibition gives rise to the deficit of cytoplasm. Since no shortages in total volumes of structural cytoplasm components were found the number and volume of mitochondria were shown even largely increased, it is assumed that asynchrony during light-induced mitotic reactivation originates from quantitative differences of constituents within the area of ground cytoplasm.
{"title":"Heterogeneity of the early G2 phase-arrested cells; cytophotometric, interferometric, and EM morphometric studies.","authors":"J Maszewski, M Kwiatkowska","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cells of antheridial filaments in Chara vulgaris L. blocked at the early G2 phase by a 5 day dark treatment were studied cytologically in order to determine causes of their heterogeneous response to light-induced mitotic activation. Cell size distribution patterns in dark inhibited populations were shown to be nearly consistent with those found within the control populations, comprising all the stages of interphase; cells which resume divisions in response to photoinduction attain, however, sizes characteristic of mitosis occurring in natural light conditions. Cytophotometric determinations of nuclei in cells given dark treatment indicated a complete homogeneity of populations in respect of replicated DNA contents. As evidence by nucleus-cytoplasm surface relations, interferometric measurements of their dry mass contents, and EM stereometric studies, the heterogeneity of early G2 phase arrested populations results from an imbalance between nuclear DNA-division cycle, which is continued up to the early stage of the G2 period, and the growth cycle, which in turn, due to its pronounced inhibition gives rise to the deficit of cytoplasm. Since no shortages in total volumes of structural cytoplasm components were found the number and volume of mitochondria were shown even largely increased, it is assumed that asynchrony during light-induced mitotic reactivation originates from quantitative differences of constituents within the area of ground cytoplasm.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"20 3-4","pages":"171-88"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18176069","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}
Using solubilization with bromelain, the light form of gamma-glutamyltransferase was purified from Morris hepatoma 5123D. Some properties of this enzyme were compared to those of the light form rat kidney GGT. Anthglutin and its isomer inhibit competitively the former enzyme but non-competitively the latter. On zymograms of rat control sera, five GGT fractions were noted, but in sera of rats with hepatoma 5123D also the light form and the increase of GGT activity ain region of fraction II were observed. Only these two enzyme fractions react with antibody anti heavy form of Morris hepatoma GGT.
{"title":"Light form of Morris hepatoma gamma-glutamyltransferase.","authors":"A Szewczuk, H Milnerowicz, E Prusak, Z Albert","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Using solubilization with bromelain, the light form of gamma-glutamyltransferase was purified from Morris hepatoma 5123D. Some properties of this enzyme were compared to those of the light form rat kidney GGT. Anthglutin and its isomer inhibit competitively the former enzyme but non-competitively the latter. On zymograms of rat control sera, five GGT fractions were noted, but in sera of rats with hepatoma 5123D also the light form and the increase of GGT activity ain region of fraction II were observed. Only these two enzyme fractions react with antibody anti heavy form of Morris hepatoma GGT.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"20 1-2","pages":"25-33"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17247366","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}
Rat and mouse parotid acinar cells have been dispersed into small acinar groups and individual cells. Amylase release in response to secretagogues has been determined. Cytochemical localization of adenylate cyclase in these cells has demonstrated isoproterenol-stimulated adenylate cyclase in the same location as the reported in tissue slices, at the extracellular aspect of the lumenal plasma membrane: adenylate cyclase activity was also visualized in completely separate cells, restricted to the lumenal pole of the cell. These results support the validity of other localizations of this enzyme in intact tissue blocks, and illustrate cytochemical similarity of cells in dispersed preparations to cells in tissue slices. The specialized location of plasma membrane adenylate cyclase at the locus of secretory granule exocytosis is retained even without intercellular junctions.
{"title":"Cytochemical adenylate cyclase: localization in dispersed parotid acinar cells.","authors":"C J Farnham, E L Watson, W F Farnham","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Rat and mouse parotid acinar cells have been dispersed into small acinar groups and individual cells. Amylase release in response to secretagogues has been determined. Cytochemical localization of adenylate cyclase in these cells has demonstrated isoproterenol-stimulated adenylate cyclase in the same location as the reported in tissue slices, at the extracellular aspect of the lumenal plasma membrane: adenylate cyclase activity was also visualized in completely separate cells, restricted to the lumenal pole of the cell. These results support the validity of other localizations of this enzyme in intact tissue blocks, and illustrate cytochemical similarity of cells in dispersed preparations to cells in tissue slices. The specialized location of plasma membrane adenylate cyclase at the locus of secretory granule exocytosis is retained even without intercellular junctions.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"20 3-4","pages":"141-51"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18177157","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}
Some hydrolases are localized cytochemically in the pollen and pollen tubes of Amaryllis vittata Ait. The function of different enzymes is discussed in relation to pollen tubes morphogenesis. Activity of most of the enzymes was confined to colpus region, pollen wall and general cytoplasm of pollen and pollen tube. The activity of hydrolytic enzymes like acid monophosphoesterase and lipase and was nil in the exine of both germinated and ungerminated pollen, whereas intense reaction for esterase was observed in exine. Enzyme activity increased after germination which suggest the hydrolysis of stored metabolites and synthesis of proteins and other metabolites for the active growth of pollen tube. Intense reaction for enzymes like alkaline phosphomonoesterase, ATP-ase, 5-nucleotidase etc. at the tip region of pollen tube suggest their role in physiological processes associated with exchange of materials through intercellular transport during tube wall polysaccharide biogenesis.
{"title":"Cytochemical localization of some hydrolases in the pollen and pollen tubes of Amaryllis vittata Ait.","authors":"D Sharma","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Some hydrolases are localized cytochemically in the pollen and pollen tubes of Amaryllis vittata Ait. The function of different enzymes is discussed in relation to pollen tubes morphogenesis. Activity of most of the enzymes was confined to colpus region, pollen wall and general cytoplasm of pollen and pollen tube. The activity of hydrolytic enzymes like acid monophosphoesterase and lipase and was nil in the exine of both germinated and ungerminated pollen, whereas intense reaction for esterase was observed in exine. Enzyme activity increased after germination which suggest the hydrolysis of stored metabolites and synthesis of proteins and other metabolites for the active growth of pollen tube. Intense reaction for enzymes like alkaline phosphomonoesterase, ATP-ase, 5-nucleotidase etc. at the tip region of pollen tube suggest their role in physiological processes associated with exchange of materials through intercellular transport during tube wall polysaccharide biogenesis.</p>","PeriodicalId":75854,"journal":{"name":"Folia histochemica et cytochemica","volume":"20 3-4","pages":"133-9"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17359659","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}