Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement最新文献

{"title":"The anal transitional zone.","authors":"C Fenger","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The macroscopical appearance of the human anal canal was first described by Glisson (1597-1677) and Morgagni (1717), who mentioned the anal valves and anal columns, respectively. The first detailed light microscopic description of the three anal canal zones originates from Robin & Cadiat (1874). The present definition of the anal canal, extending from \"the pelvic floor to the anal opening\" was suggested by Symington (1888). There are no generally accepted names for the three epithelial zones of the anal canal. A review of the literature shows that no less than three different names have been used for the upper zone, 14 for the middle zone and 9 for the lower zone, as well as 10 names for the line comprising the anal valves and the base of the anal columns. In the present work the middle zone is termed the anal transitional zone (ATZ), and is defined as \"The zone interposed between uninterrupted colo-rectal type mucosa above and uninterrupted squamous epithelium below, irrespective of the type of epithelium present in the zone itself\". The line corresponding to the anal valves and anal sinuses is termed the dentate line (DL), as this name seems to be employed in more common textbooks. The location and extent of the ATZ has previously been measured by light microscopy on a small number of sections from a few anal canals. In the present work the extent of the zone has been elucidated from a large material, where macroscopic demonstration of the zone has been carried out by means of staining with Alcian dyes on fixed surgical specimens, by stereomicroscopy and finally by light microscopic control of both methods, achieved by systematic sectioning of the specimens. The results have shown that normally the ATZ reaches from the DL and almost 1 cm upward, but that it can be observed over a considerably larger area than previously reported, namely from 0.6 cm below to 2.0 cm above the DL, and eventually may be absent altogether. Further, it has been shown that the ATZ frequently has a map-like appearance. Light microscopically, the major part of the ATZ consists of a characteristic epithelium, which is provisionally termed the ATZ-epithelium. This appears to be composed of 5-9 cells layers. The surface cells can be columnar, cuboidal or somewhat more flattened. In the first case, signs are often seen of some mucin-production.(ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"289 ","pages":"1-42"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14673631","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":"Trends in cancer incidence in the Nordic countries. A collaborative study of the five Nordic Cancer Registries.","authors":"T Hakulinen,&nbsp;A Andersen,&nbsp;B Malker,&nbsp;E Pukkala,&nbsp;G Schou,&nbsp;H Tulinius","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Time trends and differentials in cancer incidence in the five Nordic countries, Denmark, Finland, Iceland, Norway and Sweden, were investigated, using material collected by the cancer registries in each country. The incidence at all sites combined and at 23 anatomical sites was studied by age, birth cohort and time period. The maximum lengths of the trends were used for each country. In Denmark the material comprised all the tumours diagnosed in 1943-1980, in Finland and Norway those diagnosed in 1953-1980, in Iceland those diagnosed in 1955-1980, and in Sweden those diagnosed in 1958-1980. For males the age-adjusted cancer incidence rates at all sites combined were highest in Denmark and Finland, and lowest in Sweden and Norway. In females the incidence was highest in Denmark and Iceland, and lowest in Finland. The rates increased slightly for both sexes. For cancer of the pancreas, Hodgkin's disease, acute leukaemia and childhood cancer (all sites combined) the rates in all the Nordic countries were similar every year. For cancers of the stomach, colon, breast, corpus uteri, ovary, prostate, testis, urinary bladder, melanoma of the skin and non-Hodgkin's lymphomas the trends were similar but on different levels. For cancers of the larynx and lung in males the rates in Finland decreased during the 1970s, whereas the rates were increasing in the other Nordic countries. For cancer of the rectum, the trend showed a decrease in Denmark but an increase in the other Nordic countries. For lip cancer the rate in Sweden was almost constant over time, but in Denmark, Finland and Norway a decrease occurred. For oesophageal cancer in males the rates decreased in Finland and Iceland in the 1970s, whereas in Denmark and Norway there was very little change, and in Sweden there was an increase in the rates. For cancer of the cervix uteri the rates started to decrease in Denmark, Finland, Iceland and Sweden in the mid-1960s, but in Norway not until some ten years later. The differentials between the countries were largest for cancers of the testis and thyroid, in which the highest incidence was five to six times as large as the lowest. For testicular cancer the rate was the highest in Denmark, for thyroid cancer in Iceland. For both of these cancers the rate was the lowest in Finland. Melanoma of the skin was the cancer with the most rapid increase in incidence with time in all the Nordic countries.(ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"288 ","pages":"1-151"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14589621","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":"Aleutian disease of mink. Virology and immunology.","authors":"B Aasted","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"287 ","pages":"1-47"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14133445","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":"Immunomodulatory effects of interferons on human mononuclear cells with special reference to the expression of cell surface antigens.","authors":"M E Hokland","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"286 ","pages":"1-35"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13557609","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":"Cold enhancement of blood coagulation: observations on the role of C1(-)-inhibitor.","authors":"V H Donaldson","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The effect of incubation at 4 degrees C upon the one stage prothrombin times and the Thrombotest times of plasma from normal people, females taking oral contraceptive agents (O.C.A.'s) or in the third trimester of pregnancy, and patients with hereditary angioneurotic edema (H.A.N.E.) was measured to determine if enhancement of coagulant activity was regularly associated with reduced amounts of C1(-)- inhibitor (C1(-)-INH) in the plasma. Cold-enhanced coagulant activity was not always found in H.A.N.E. plasmas, markedly deficient in C1(-)- INH, and when found, the addition of purified C1(-)-INH to the plasma did not always prevent its development in vitro. Females taking O.C.A.'s regularly demonstrated cold-enhanced plasma coagulant activity in this series, as did pregnant females tested, as reported by others. The relation of C1(-)-INH levels in plasma to the cold-enhanced plasma coagulant activity was imperfect. In plasma obtained during pregnancy, but not exposed to 4 degrees C, C1(-)-INH levels were low despite minimal shortening of the Thrombotest time. Thus, these observations suggest that reduced levels of C1(-)-INH in plasma was not directly related to the tendency to generate enhanced coagulant activity at 4 degrees C. Other factors must be critical to the development of this activity, and the failure to block its development in C1(-)-INH deficient plasmas by adding purified C1(-)-INH at venesection suggests that events which initiate the development of this property may have occurred in vivo.</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"284 ","pages":"41-7"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17643711","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":"Generation of the classical pathway C3 convertase (EAC4b2a) by proteolytic enzymes.","authors":"M Loos,&nbsp;H P Heinz","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The formation of EAC 4b2a is a two step reaction: first, the temperature- and time-independent binding of C2 to EAC4b2a resulting in EAC4b2 , secondly, the enzymatically triggered conversion of EAC4b2 to EAC4b2a . In the classical cascade of complement activation, the generation of C3 convertase activity is triggered by the C1 esterase, C1-s, which is part of C-1. Evidence is presented that the enzymes trypsin, chymotrypsin, plasmin, and pronase are also able to activate EAC4b2 to EAC4b2a . Kinetic studies showed that the formation of C3 convertase by these enzymes was dependent on concentration, temperature, and time. The optimal conditions were found as follows: trypsin, 2 micrograms/ml (final conc.) for 8 min at 23 degrees C; chymotrypsin 165 micrograms/ml for 18 min at 23 degrees C; plasmin 0.8 units/ml for 15 min at 23 degrees C; pronase 1.25 microgram/ml for 15 min at 23 degrees C. Even under optimal (tmax) conditions the number of generated EAC4b2a differed from enzyme to enzyme: trypsin (= 100%), pronase (58.3%), chymotrypsin (47.9%), and plasmin (12.9%). The enzymes were also able to generate C3 convertase activity from C2 which was adsorbed to EAC1i4b , a C1 inactivator treated and therefore hemolytically inactive intermediate ( EAC1i4b2 ). These findings underline the biological importance of C1 esterase replacing enzymes.</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"284 ","pages":"67-74"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17435209","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 C1q with beta 2-microglobulin.","authors":"L Björck,&nbsp;U Johnson,&nbsp;A G Sjöholm","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Beta 2-microglobulin aggregated with glutaric dialdehyde was efficiently bound to C1q in fluid and solid phase assay systems. Furthermore, affinity chromatography experiments suggested reactivity of monomeric beta 2-microglobulin with C1q. In spite of its C1q binding capacity, the aggregated beta 2-microglobulin did not activate the C1 complex in serum. This however, might have been due to the mode of aggregation.</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"284 ","pages":"19-23"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17435326","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":"Freeze-thaw activation of the complement attack phase: I. Separation of two steps in the formation of the active C--56 complex.","authors":"A Dessauer,&nbsp;U Rother,&nbsp;K Rother","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The activation of the attack phase of C, C5-C9, is generally assumed to be dependent on the enzymes of the C activation pathways which cleave C5 into C5b and C5a. C5b will then form a complex with C6 that binds to membranes and, in the presence of C7-C9, effects cell lysis. In contrast, however, a variety of physicochemical means was found to activate C5 + C6 independently of the convertases and without apparent generation of the C5a peptide. By freezing and thawing of C5 + C6 a hemolytic C--56 activity was generated: (C--56 ).f The activation proceeded in two steps: (1) during a preincubation period of the two components the time and temperature dependent formation of an activatable intermediate was observed and (2) the intermediate C--56 could then be endowed with hemolytic activity by freezing and thawing. The intermediate as well as the activated (C--56)f complex was separated from C5 and C6 by anion exchange chromatography. While the isolated intermediate was labile, the active product after freezing and thawing was stable.</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"284 ","pages":"75-81"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17643714","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":"Location of the binding site in subcomponent C1q for plasma fibronectin.","authors":"K B Reid,&nbsp;J Edmondson","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Previous studies on the interaction of fibronectin with C1q have yielded apparently conflicting results since both the globular head regions (produced by collagenase digestion) and the collagen-like domains (produced by limited pepsin digestion) have been reported to bind to fibronectin. In this study, the binding of 125I-labelled fibronectin to either intact C1q, or the collagenase or pepsin digestion products, immobilised on plastic microtitre plates was examined. Inhibition of the C1q-fibronectin interaction by the C1q digestion products was also examined. The results confirmed that both globular 'head' region preparations and collagen-like region preparations, can interact with fibronectin. Since the fragments used in these studies share a section of common amino acid sequence from the C1q molecule it can be concluded that the binding site, on C1q for fibronectin, is located in a region formed from the residues 81-97 of each of the three chains of the C1q molecule.</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"284 ","pages":"11-7"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17666228","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":"Evidence of persistent IgA/IgG circulating immune complexes associated with activation of the complement system in serum of a patient with common variable immune deficiency: anaphylactic reactions to intravenous gammaglobulin.","authors":"V Wahn,&nbsp;R A Good,&nbsp;S Gupta,&nbsp;S Pahwa,&nbsp;N K Day","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A 44 year old woman with common variable immunodeficiency developed severe anaphylactic reactions to intravenous gammaglobulin. Analysis of her serum prior to the infusion of gammaglobulin was thus analyzed and the tests revealed a complete absence of free IgA, presence of an IgG autoantibody to IgA, IgA-IgG circulating immune complexes, and depressed levels of hemolytic C3 associated with elevated levels of C3a and C3d. The IgA-IgG complexes did not clear from the circulation even after six months following cessation of gammaglobulin infusions. Analysis of the complexes isolated by sucrose density gradient ultracentrifugation showed that they bind to solid phase F(ab')2 anti-C1q, have a high molecular weight (greater than 19s), activate the complement (C) system via the classical pathway in vitro and are comprised of IgG and IgA. These data suggest that in this patient an autoantibody response to IgA was probably associated with persistent endogenous production of IgA yielding IgG-IgA circulating immune complexes and activation of the complement system. Although the patient has no free IgA and no surface IgA bearing B cells, her peripheral blood lymphocytes were shown to contain cells capable of secreting IgA. Low levels of IgM and IgG were detectable in her serum, and B cells bearing surface IgM, IgG and IgD were present in normal numbers in the blood.</p>","PeriodicalId":77654,"journal":{"name":"Acta pathologica, microbiologica, et immunologica Scandinavica. Supplement","volume":"284 ","pages":"49-58"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17267290","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}