Generally, fate of spematogonial stem cells (SSCs) can be determined specifically by microenvironments enclosed with various extracellular matrix (ECM) components and integrins recognizing directly ECM proteins play an pivotal role in transporting ECM-derived signals into cytoplasm, resulting in inducing a variety of biological functions such as cell attachment, self-renewal and differentiation. However, to date, studies on type of integrins expressed on the undifferentiated SSCs remain unclear. Therefore, we tried to investigate systematically what kind of integrin subunits are expressed transcriptionally or translationally in the SSCs derived from testis of hybrid B6CBAF1 mouse. For these, isolation of SSCs from testis were conducted by magnetic activated cell sorting (MACS) using Thy1 antibody. Subsequently, transcriptional and translational level of integrin α and β subunits in the isolated SSCs were measured by real-time PCR and fluorescene immunoassay, respectively. As the results, transcriptional levels of genes encoding total 25 integrin subunits were quantified, and integrin α4, α6, α7, α9, αV, αL and αE and integrin β1, β5 showed higher expression levels than other subunits. By contrast, integrin α3, α5, α 10 and α11 and integrin β2, β3, β4, β7 were weakly transcribed. When translational levels of the integrin α subunits showing high transcription level (α4, α6, α7, α9, αV αL, and αE) were measured, integrin α6, α7, α9, αV and αL were higher than integrin α4 and αE. In case of integrin β subunit, β1 evaluated more expression than β5. From these results, we speculate that the undifferentiated SSCs derived from hybrid B6CBAF1 mouse may express integrin α4β1, α6β1, α7β1, α9β1, αVβ1 and/or αVβ5 on plasma membrane. Moreover, this information will greatly contribute to constructing non-cellular niche supporting self-renewal of SSCs in the future.

Integrin is a cell surface protein that is composed of α and β heterodimer and mediates cell interaction with extracellular matrix or other cells including microbial pathogens. A full length cDNA sequence (2,517 bp) of a integrin subunit β1 (HaITGβ1) was cloned from the oriental tobacco budworm, Helicoverpa assulta. Phylogenetic analysis showed that HaITGβ1 was clustered with other insect β integrin subunits with the highest amino acid sequence identity (61%) to β1 of other Noctuidae such as Spodoptera exigua and S. litura. Structural analysis of the HaITGβ1 possessed all functional domains known in other insect β1 integrins. RT-PCR analysis showed that HaITGβ1 was expressed in all developmental stages and all tested tissues of H. assulta. Injection of double-stranded HaITGβ1 RNA (dsHaITGβ1) into third instar of H. assulta suppressed HaITGβ1 expression and resulted in significant delay from last larval stage to pupal stage. The dsHaITGβ1 injection significantly impaired nodule formation of H. assulta in response to bacterial challenge and hemocyte adherence. These results suggest that HaITGβ1 plays crucial roles in cellular immune responses as well as development in H. assulta.

The purpose of this study was to evaluate the role of integrin α3 and integrin β1 in the ameloblastomas. For this study, 10 specimens diagnosed as amoblastomas referred to the Department of Oral Pathology, School of Dentistry, Kyung Hee University, and 5 specimens of normal oral mucosa without any inflammatory changes were used as experimental and control groups, respectively. The ameloblastomas devided into follicular type, plexiform type, acanthomatous type, and granular cell type. All specimens; experimental and control group were fixed in 10% neutral formalin solution and embedded in paraffin, and then the serial tissue sections were made 5㎛ in thickness and processed for immunohistochemical observation. The specimens were incubated with primary antibody against integrin α3 or integrin β1, each was diluted at 1 : 100, followed by the Supersensitive non-biotin horse radish peroxidase detection system with DAB as chromogen. After counterstaining with Gill's hematoxylin stain method and mounted, and examined under the light microscope. Based on the intensity of the immunoreactivity, intensity of the immunity was scored no epithelial stain, weak or focal epithelial stain, moderate or focal intensive epithelial stain, intense generalized epithelial staining for the epithelial, and connective tissue component in ameloblastomas, and normal oral mucosa on each. Attained results as follows. Expression of integrin α3 in the oral mucosa, weak reaction was noted on the all layers of epithelium, and submucosa. Expression of integrin β1 in the oral mucosa, intense reaction on the superficial layer, moderate reaction in basal layer were shown. Expression of integrin α3 in ameloblastomas, it was noted that weak reaction on the ameloblast like cells in the all types and rarely in basement membrane. Expression of integrin β1 in ameloblastomas, intense reaction on the tumor cell ,and partly in the nuclei in follicular type was noted, And moderate reaction on the tumor cell in plexiform , acathomatous types, but weak reaction in granular cell type was shown. This results result suggest that integrin α3 may influenced negligibly, but the integrin β1 influenced significantly the development of the ameloblastomas considering the response is increased on the region with highly cellular activities

The purpose of this study was to evaJ uate the role of integrin a 3 and integrin ß 1 expression in the saivary gJand tumors. For this study, 11 specimens diagnosed as pleomorpic adenoma, adenoid cystic carcinoma, adenocarcinoma, mucoe pidermoid carcimoma referred to the Dept. of Oral Pathology‘ School of Dentistry, Kyung Hee University, 2 specimens 01' normaJ submandibular gland tissues were used as experimental, control groups respectively, All the tissues experimental and control group wel'e fixed in neutral formaJin solution and embedded in paraffin, seriaJ tissue section were made 511m in thickness and processed in the standard way for immunohistochemical method, using primary antibody against integrin a 3, and integrin ß 1 each was diluted at 1;100 followed by the poly- horse radish peroxidase detection system with DAB as chormogen counterstained with Mayel ’s hematoxylin stain method and mounted And examined unde1' the biologic micro scope with the criteria of no epitheliaJ stain, weak 01' focal epithelial stain, moderate 01' focal intensive epithelial s tain. intense generalized epithelial staining for the epithelial, and connective tissue components in no1'mal salivary gland, and saivary g land tumors : pleomorphic adenoma‘ adenoid cystic carcinoma, adenoca1'cinoma, mucoepide1'moid ca1'cinoma on each On the integ1'in α 3 reaction, negative to minimal posit ive reaction was noted on the salivary gland twnors and nor mal subma ndibular gland tlssues On the integrin ß 1 reactions, intense 1'eaction is shown on the serous demilune and ductal cells , and partly on the serous acini in submandibula1' gland tlssues On the integrin ß 1 reactions to pleomorphic adenoma tissues, moderate reactions were noted on the ductal celJs and myoepithelial cells. On the integrin ß 1 reactions to adenoid cystic ca rci noma‘ adenocarcinoma, mucoepidermoid ca1'cinoma tissues, intense reactions were shown on the neo plastic cell s , This resuJt suggest that integrin a 3. integrin ß 1 could be a 1'ole inducing the tumorigenesis.

The purpose of this study was to evaluate the role 0 1' integrin a 3 and integrin ß 1 in the oral squamous cell ca rcinomas. For this study‘ 10 specimens diagnosed as squamous cell carcinoma referred to the Dept. of Oral Pathology. School of Dentis try, Kyung Hee Univers ity, and 5 specimens of normal oral mucosa without any inflammatory cha nges were used as experimenta l and co nt rol groups, respectively. AlI s pecimens; experirnental and control group were f ixed in neutral f ormalin so lu tion and embedded in paraffin, and then the serial tissue section were rnade 5i1m in thickness and processed for imrnunohi stochemical observatlon The specimens were incubated with prirnary antibody against integrin a 3 r integrin ß 1‘ each was diluted at 1;100, followed by the super sensit ive non- biotin horse r adish peroxidase detection sys tem with DAB as chromogen‘ After counters ta ining with Gill ’s hematoxylin stain method and mounted and examined under the light microscope. Based on the intens ity of the immunoreactivity, intensity of the immunity was scored no ep ithelial stain, weak 0 1' focal epitheli al sta in, modera te 0 1' focal intensive epithelial stain, intense genera lized epitheli al s taining for the e pithelia l, and co nnective ti ssue component in squamous cell carcinomas, and normal oral mucosa on each Expression of integrin a 3 in t he oral mucosa was negli gible. Expression 0 1' integrin a 3 in expression in the or al s mnus cell ca rcinoma was ve ry wea k, but the express ion was increased in poorly differ entiat ed type of the oral squamous cell carcinomas ln the oral mucosa , expression of in tegr in ß 1 ra nged from weak to moderate in the cytoplasm and the cell membra nes of the kera tini zed and basal cell layer. Nuclei were mainly integrin ß 1 negative‘ but rarely revealed weak expression. ln sq uamous cell carcinoma, expression of integrin ß 1 was ntense notably in the cytoplasm, cell membrane a nd nuclear membra ne Nuclei of several tumor cells revealed moderate expression of integrin ß 1. Expression of integrin ß 1 was increased the poorly diffe rentiated type of in squamous cell carcinoma compare to that in moderate or well diffe rentiated type of oral squamous cell carCllìoma These results suggest integrin a 3 and integrin ß 1 may be influ enced the development and growth of the squamous cell carcima .