胃癌及胃壁组织内淋巴管分布的研究

本文首次用５′－Ｎａｓｅ－ＡＬＰ双重组织化学方法观察了２０例胃癌组织和癌旁胃壁组织内淋巴管的细微分布。在光镜下毛细淋巴管和淋巴管５′－Ｎａｓｅ染色强阳性,管壁显示明显的棕色或深棕色,而毛细血管和血管的ＡＬＰ反应显示强阳性,管壁呈明显的蓝色。据此可将淋巴管、血管区别开来、本研究发现胃癌组织内有较多的淋巴管、毛细淋巴管以及较多的棕色实性条状组织,这些条状物可能是新生的毛细淋巴管。上述结果为研究癌组织内淋巴管的分布及胃癌淋巴道转移,提供了可靠的实验方法。     

微小RNA-205 在甲状腺乳头状癌中的表达及临床意义

目的:观察微小RNA(microRNA,miRNA,miR)-205在甲状腺乳头状癌(PTC)中的表达并探讨其临床意义。方法:收集自2014年1月至2014年12月在我院甲状腺外科住院治疗的甲状腺乳头状癌患者的术后新鲜病理组织45例,其中男14例,女31例,年龄24-69岁,平均45.5岁。结节性甲状腺肿28例,癌旁正常甲状腺组织5例。提取各组织中的miRNA,应用实时荧光定量聚合酶链反应(RT-q PCR)方法检测miR-205的表达情况。结果:甲状腺乳头状癌miR-205的表达量较非肿瘤组织(结节性甲状腺肿、癌旁组织)明显下调[(1.06±1.76)vs(3.19±4.88),P=0.038]。伴淋巴结转移的PTC组织中miR-205表达量明显低于无淋巴结转移的PTC组织[(1.21±1.80)vs(9.59±1.60),P=0.003]。miR-205的相对表达与PTC患者性别、年龄及浸润与否均无显著相关性,而肿瘤直径呈显著相关性。结论:miR-205在PTC中的表达异常下调,可能与PTC的发生、侵袭和转移有关。     

128层螺旋CT 低剂量扫描检查孤立性肺内结节性病灶的研究

目的:探讨多排螺旋CT(128排)低剂量扫描参数下检查孤立性肺内结节的可行性研究。方法:随机连续搜集我院低剂量(30m A)CT肺体检者,发现肺内结节病灶患者13例,对其进一步以常规剂量(350m A)CT精细扫描,比较低剂量扫描及常规剂量扫描肺结节大小差异。结果:两种剂量扫描策略均检查出46枚结节。常规剂量与低剂量测得各部位结节体积分别为:肺尖部:(431.3±92.8)mm~3,(658.4±94.4)mm~3,肺中部:(3025.8±526.7)mm~3,(2989.4±520.4)mm~3,肺底部:(1241.5±438.9)mm~3,(1266.0±447.6)mm~3,肺尖部肺结节大小差异明显,肺中部及肺底部肺结节大小均无显著性差异(P0.05)。常规剂量与低剂量测得结节体积(除外肺尖部位结节5枚)分别为,组1:(39.8±14.6)mm~3,(40.7±15.5)mm~3;组2:(202±106.3)mm~3,(204.1±103.6)mm~3;组3:(4179.7±4410.4)mm~3,(4190.5±4487.2)mm~3。三组组内测量结果均无显著性差异(P0.05)。常规剂量与低剂量测得非实性结节密度[(-68.3±24.2)HU,(-64.6±22.8)HU]及实性结节结节密度[(97.5±69.5)HU,(107.2±90)HU]均无统计学差异(P0.05)。结论:低剂量更加有利于肺内孤立结节患者扫描复查病灶,可以应用推广。     

人体正常扁桃体和淋巴结T、B淋巴细胞亚群的研究

本文用了一系列T、B淋巴细胞单抗,用免疫细胞化学技术观察了人淋巴结和扁桃体内T,B淋巴细胞及其亚群。T细胞及其亚群主要位于滤泡间的副皮质。此外在淋巴结髓质也有一定数量的T细胞亚群的分布;次级滤泡生发中心也常出现辅助T或Leu 4阳性T细胞。B淋巴细胞及其亚群多集中在初级和次级滤泡,如OKB_2和BA 1阳性细胞多集中于次级滤泡的帽状区,而IgM主要位于次级滤泡的生发中心。LN-2抗体选择性地与生发中心??和帽状区的B细胞的核膜起反应,是研究B细胞表型的一种重要试剂。     

Glycosyl receptors in macrophage subpopulations of rat spleen and lymph node

Summary We have developed an immunohistochemical method for the in vivo and in vitro detection of glycosyl receptors in rat spleen and lymph nodes by using neoglycoproteins. The receptor in both organs recognized mannose coupled to bovine serum albumin (mannose-BSA), fuscose-BSA, N-acetylglucosamine-BSA and to a lesser extent glucose-BSA, but not galactose-BSA or N-acetylgalactosamine-BSA. In vitro neoglycoprotein-receptor binding was Ca²⁺ dependent and could be inhibited by mannan but not by mannose. Simultaneous staining with the monoclonal antibodies ED1, ED2 or ED3 revealed that only ED1-and ED3-positive macrophages were involved in the binding of neoglycoproteins. In the spleen, the marginal-zone macrophages and a subpopulation of the marginal metallophils possess glycosylbinding receptors. In the lymph nodes, the medullary sinus macrophages and a subpopulation of the outercortex macrophages are able to bind neoglycoproteins.     

Trypanosoma congolense. II. Histopathologic findings in experimentally infected cattle

Heart, kidney, lung, liver, brain, spleen, lymph nodes, tongue, and diaphragm of 9 cattle experimentally infected with the Trans Mara I strain of Trypanosoma congolense, were examined histologically. A haemosiderosis, infiltrations in the kidney, changes in the vascular wall mainly of the arteries of the lung, scattered local perivascular, and meningeal infiltrations, and small juxtavascular glial nodules in the CNS were found.     

The formation of “compartment replicas” in the lymph nodes of athymic animals

Summary This communication describes a new anomaly that can affect the capsule of lymph nodes of athymic animals. Lymphocytes infiltrate a segment of the capsule above the variably atrophied peripheral cortex overlying the center of the deep-cortex unit of a node compartment. Lymphocytes thereafter form a capsular mass. The developing mass of lymphocytes is invaded by outgrowths of the node's subcapsular sinus while it fuses with the parenchyma of the related node compartment. Eventually, this new nodal element acquires structures resembling those of nodes and becomes a more or less exact replica of the original node compartment. Replicas stem from node compartments that are overchallenged by uncontrolled antigens. Aspects of the formation of replicas are explained by recent findings on events occurring in nodes of athymic animals and on the pattern of antigen distribution in the subcapsular sinus of a node. It is concluded that the formation of a compartment replica constitutes a mechanism allowing the organism to compensate somewhat for the partial atrophy or deficiency of a node compartment.Work funded by the Medical Research Council of Canada     

Regeneration of autotransplanted lymph node fragments

Summary In normal young minipigs thin slices of autologous mesenteric or superficial inguinal lymph nodes were implanted either in the greater omentum or subcutaneously in the groin region. The regeneration was studied histologically and connections between the afferent lymphatics and the regenerated tissue were checked. In the greater omentum, no regenerated lymph node tissue was found. In the inguinal region, lymphoid tissue with all the typical lymph node compartments was identified following antigenic stimulation in the draining area. Sinuses, germinal centres with a lymphatic corona, and a paracortex with typical high endothelial venules were seen. There was evidence of afferent lymphatics, e.g., macroscopically visible lymphatics, the occurrence of a subcutaneously injected dye, the effect of antigenic stimulation and a normal lymph node structure. Avascular transplants of autologous lymph node fragments regenerate subcutaneously, possibly providing a future technique for treating lymphoedema after radical excision or irradiation of lymph nodes.     

Precise localization of antigens on follicular dendritic cells

Summary Horse-spleen ferritin or bovine serum albumin conjugated to colloidal gold (BSA-gold) were injected subcutaneously in preimmunized mice. In draining lymph nodes both antigens were located in macrophages or between the cytoplasmic processes of follicular dendritic cells (FDC). Some of the antigens remained trapped on FDC until day 31 after injection. Simultaneous injection of both antigens showed that they were located between the infoldings of the same FDC. These cells are thus able to retain at least two different antigens on their surface. The peculiar arrangement of ferritin between the cytoplasmic infoldings suggests that this antigen is fixed on both cell membranes by specific antibodies. The trapped immune complexes could thus stabilize the FDC membrane system.The antigen retention requires the presence of specific antibodies since BSA-gold or ferritin injected without preimmunization were not found between FDC processes. Nonantigenic materials, such as colloidal gold or carbon particles, are not trapped by FDC, except when injected in large amounts.The antigens were trapped on the surface of FDC, however unfrequently in close contact with lymphocytes. FDC might protect lymphocytes against an excess of immune complexes and act as regulators of contacts between lymphocytes and immune complexes.Abbreviations BSA bovine serum albumin - BSA-gold BSA conjugated to colloidal gold particles - FDC follicular dendritic cells     

CD69 Suppresses Sphingosine 1-Phosophate Receptor-1 (S1P1) Function through Interaction with Membrane Helix 4

Lymphocyte egress from lymph nodes requires the G-protein-coupled sphingosine 1-phosphate receptor-1 (S1P₁). The activation antigen CD69 associates with and inhibits the function of S1P₁, inhibiting egress. Here we undertook biochemical characterization of the requirements for S1P₁-CD69 complex formation. Domain swapping experiments between CD69 and the related type II transmembrane protein, NKRp1A, identified a requirement for the transmembrane and membrane proximal domains for specific interaction. Mutagenesis of S1P₁ showed a lack of requirement for N-linked glycosylation, tyrosine sulfation, or desensitization motifs but identified a requirement for transmembrane helix 4. Expression of CD69 led to a reduction of S1P₁ in cell lysates, likely reflecting degradation. Unexpectedly, the S1P₁-CD69 complex exhibited a much longer half-life for binding of S1P than S1P₁ alone. In contrast to wild-type CD69, a non-S1P₁ binding mutant of CD69 failed to inhibit T cell egress from lymph nodes. These findings identify an integral membrane interaction between CD69 and S1P₁ and suggest that CD69 induces an S1P₁ conformation that shares some properties of the ligand-bound state, thereby facilitating S1P₁ internalization and degradation.