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T Saku

Publications and source records attributed to T Saku.

At least 73 records · Page 4Linked to original sources
PubMed1989

Quantitation and immunohistochemical localization of cathepsins E and D in rat tissues and blood cells.

The distribution of cathepsins E and D in various rat tissues and blood cells was determined by immunoprecipitation and by immunohistochemistry with discriminative antibodies specific for each enzyme. While cathepsin D was detected in all of the tissues and blood cells tested (except for erythrocytes), cathepsin E had a relatively limited distribution. The cathepsin E content was highest in the stomach and was succeeded in the following order by the urinary bladder, thymus, spleen, cervical lymph node and bone marrow. Significant amounts of cathepsin E were also found in the colon, rectum, jejunum, skin, lung, kidney and submandibular gland. The other tissues tested had little or no detectable cathepsin E content. Of the blood cells tested, lymphocytes and peritoneal neutrophils contained high levels of cathepsin E. Erythrocytes had cathepsin E only as aspartic proteinases. When the subcellular localization of cathepsin E in the neutrophils was investigated by fractionation of the postnuclear supernatants, the enzyme behaved as a soluble cytosolic enzyme. In contrast, cathepsin D was mainly associated with the granular fraction. The immunohistochemical localization of cathepsins E and D was clearly different in the stomach, large intestines, kidney and urinary bladder, but was similar in the lymph node and spleen. The tissue-fixed macrophages, which were notable in the skeletal and cardiac muscle tissues, submucosal layers of the gastrointestinal tracts, salivary gland, lung and trachea, also exhibited similar intense immunoreactivities demonstrative of both cathepsins E and D.

Acid Phosphatase↗
PubMed1989

Characterization of the major heparan sulfate proteoglycan secreted by bovine aortic endothelial cells in culture. Homology to the large molecular weight molecule of basement membranes.

To determine the precise architecture and functional characteristics of the subendothelial basal lamina, detailed information of the molecules contained in this structure is required. To this end, we have studied low passage bovine aortic endothelial cells and have isolated the major heparan sulfate-containing proteoglycan from the growth medium of the cells maintained under static culture conditions. This large macromolecule consists of a core protein approximately 500,000 daltons in mass and two to three glycan side chains as revealed by carbon/platinum rotary shadow casting. Specific antibodies raised by immunization of rabbits with the native or deglycosylated bovine molecule could be isolated from an immunoadsorption column prepared with a preparation isolated from the murine Engelbreth-Holm-Swarm tumor. The antibodies purified by immunoaffinity react with basement membranes of blood vessels, lung, liver, or skin, and this reactivity is indistinguishable, at least for the organs studied, from the reactivity of antibodies specific for the Engelbreth-Holm-Swarm tumor-derived high molecular weight heparan sulfate proteoglycan isolated previously. Immunoelectron microscopy of frozen ultrathin tissue sections from the kidney indicates localization of the epitope(s) also in the basement membranes of the renal glomeruli and tubuli. The close structural relationship and homology between the aortic endothelial cell product can be demonstrated even more convincingly by two-dimensional peptide mapping procedures. The peptide patterns from the bovine and mouse products of approximately 500 kDa are nearly indistinguishable. Maps of polypeptides of molecular masses ranging from 400 to 150 kDa, which are found in the bovine as well mouse tumor preparation, are clearly related to each other and suggest that this proteoglycan is quite sensitive to degradation by tissue proteases. Thus the data presented here strongly suggest that the large proteoglycan previously isolated and described as a tumor cell product can be produced by normal cells.

Amino Acids↗
PubMed1989

Differential lectin-bindings in normal and precancerous epithelium and squamous cell carcinoma of the oral mucosa.

In order to establish a useful and objective marker of malignancy of oral mucosa, the binding sites for Ulex europaeus agglutinin I (UEA-I). Bandeiraea simplicifolia agglutinin I (BSA-I) and peanut agglutinin (PNA) were comparatively examined in the surgical materials from the normal, dysplastic and cancerous epithelium of the oral mucosa by a novel lectin-antilectin immunoperoxidase method. Based on the staining patterns of the normal keratinized epithelium, UEA-I was regarded as the marker for the prickle cells, BSA-I for the cells in the upper prickle to the horny layers, and PNA for those in the basal layer. As the degree of dysplasia advanced, all layers of epithelium came to react with UEA-I and PNA, whereas the BSA-I binding was negative. Positive reactions for UEA-I and PNA were seen in most carcinoma cells other than the keratinizing foci stained by BSA-I. The results indicate that a UEA-I-positive reaction in the basal cells, a PNA-positive in the prickle cells and loss of receptor for BSA-I occur in the course of malignant transformation of oral mucosa, and that these lectins may be regarded as useful markers of oral epithelial cytoplasmic differentiation.

Carcinoma, Squamous Cell↗
PubMed1986

Inhibition of laminin self-assembly and interaction with type IV collagen by antibodies to the terminal domain of the long arm.

Laminin is a major glycoprotein of the basement membrane. Although its precise localization and orientation within this structure is unknown, it is presumably anchored to other macromolecules such as type IV collagen or proteoheparan sulfate. In vitro, laminin has the ability to self-assemble and to bind to type IV collagen molecules at distinct sites. To identify more precisely the domains of the complex, cross-shaped laminin molecule that are involved in these interactions, images of laminin-laminin dimers and laminin-type IV collagen complexes obtained by the rotary shadowing method were analyzed. We observed that the complex domain at the end of the long arm of laminin is predominantly involved in these interactions. By using Fab fragments of antibodies specific for a peptide fragment derived from this complex domain, it is shown that laminin self-assembly is inhibited in their presence, as measured by turbidity and by electron microscopy. In addition, these antibodies inhibit the specific interaction of laminin with type IV collagen. These data suggest that the complex domain at the end of the long arm of laminin contains binding sites of potential importance for the assembly of basement membranes.

Animals↗
PubMed1986

Infantile myofibromatosis. Report of two cases.

Two cases of infantile myofibromatosis were presented. Case 1 was a 6-month-old girl with multiple nodular lesions in the left parietal bone, dermis of abdominal wall, chest wall, right upper arm, and bilateral femur. Case 2 was a 12-month-old girl with solitary nodular lesions in the left parietal bone having a tendency to enlarge. Histologically, these tumorous lesions consisted of broad bundles of well oriented spindle-shaped cells superficially resembling smooth muscle tissue. In electron microscopy, the constituent cells combined ultrastructural characteristics of both fibroblasts and smooth muscle cells., Immunoperoxidase method showed that anti-smooth muscle antibodies binded to the cytoplasm of the bundle forming cells. From these results, it may be concluded that the lesion consisted of pure proliferation of myofibroblasts, and its peculiar growth behavior was discussed, though the histogenesis still remains obscure.

Female↗
PubMed1986

The localization of human keratin proteins at cytological and histological levels in carcinomatous and sarcomatous lesions.

Immunoperoxidase staining for human keratin proteins was performed cytologically on samples from 90 patients with malignant tumors, and histologically on samples from 164 patients with malignant tumors. At the cytological level, almost all tumor cells not only in squamous cell carcinoma but also in nonsquamous cell carcinoma were positive for keratin proteins, in contrast with the apparent abscence of keratin proteins in sarcoma. At the histological level, almost all neoplastic cells of squamous cell carcinoma were positive for keratin proteins, the same as at the cytological level. In contrast, among cases of nonsquamous cell carcinoma, the frequency of appearance of keratin proteins varied according to the organ; it tended to be low in tumors with relatively good prognosis, such as carcinomas in the digestive system or thyroid cancer, and to be high in tumor with poor prognosis, such as pulmonary cancer, gallbladder cancer and endometrial cancer. However, there was a marked difference between the frequency of appearance of keratin proteins at the cytological level and that at the histological level, particularly in the cases of gastric cancer.

Antibodies↗
PubMed1985

The localization of cytoskeletal proteins and thyroglobulin in thyroid microcarcinoma in comparison with clinically manifested thyroid carcinoma.

A comparative study was performed by the use of immunoperoxidase staining of 11 cases of thyroid microcarcinoma and 7 cases of clinically manifested thyroid carcinoma. Antibodies against four kinds of cytoskeletal proteins and thyroglobulin were used. In both the microcarcinoma and manifested carcinoma groups, actin and myosin were found in almost all neoplastic cells of all patients, and keratin and vimentin were present in the tumor cells of several patients. Keratin was found only in papillary carcinoma cells. Thyroglobulin was present in the neoplastic cells of several patients from each group; follicular carcinoma cells and keratin-negative cells reacted more strongly with thyroglobulin than did papillary carcinoma cells or keratin-positive cells. There was no special difference between microcarcinoma and clinically manifested carcinoma in the location of cytoskeletal proteins and thyroglobulin.

Actins↗
PubMed1985

[Immunohistochemical localization of cytoskeletal proteins and thyroglobulin in the follicular cells of Hashimoto's thyroiditis].

Using antisera against three kinds of cytoskeletal proteins (keratin proteins, actin protein and myosin protein) and thyroglobulin, immunoperoxidase staining was performed on the follicular cells of 30 patients with Hashimoto's thyroiditis. These patients were subdivided into three types by Woolner's classification: 9 patients of lymphoid type (L-type), 12 patients of oxiphilic cell type (O-type), and 9 patients of pronounced epithelial destruction type (P-type). The results obtained were as follows: (1) In three-ninths to seven-twelfths of the patients of O-type and P-type, the cytoskeletal proteins were identified in the epithelial cells forming degenerating or atrophic thyroid follicles. In the patients of L-type, however, the cytoskeletal proteins which form large follicles containing much colloid were not found in the epithelium. (2) In some patients of O-type, keratin proteins were abundantly present in the epithelial cells with squamous cell metaplasia. (3) In the patients of L-type, thyroglobulin was found in most of the epithelium forming large follicles, but it was not found in those forming degenerating or atrophic follicles in the patients of O-type and P-type.

Adult↗
PubMed1985

Glomus tumor of the cheek: an immunohistochemical demonstration of actin and myosin.

A rare case of a buccal glomus tumor was examined by light and electron microscopy. Histologically, the tumor consisted of various vascular spaces surrounded by masses of epithelioid glomus cells, coexisting with a hemangiomatous proliferation of the vessels. Immunohistochemical stainings revealed that the tumor cells were positive for smooth-muscle actin and myosin, with various intensities of the stainings. The electron microscope invariably showed microfilaments in the tumor cells. The results suggest that the glomus tumor cells have characteristics of the smooth-muscle cell and the tumor has a hamartomatous nature.

Actins↗
PubMed1985

Smooth and skeletal muscle myosins in spindle cell tumors of soft tissue. An immunohistochemical study.

Histological localization of myosins of the smooth and skeletal muscles was investigated in comparison with that of myoglobin by immunoperoxidase technique using the antibody against each of them in surgical specimens from spindle cell tumors and tumor-like lesions of the soft tissue. Skeletal muscle myosin was demonstrated in all of the cases of rhabdomyosarcoma, whereas myoglobin was found in 75% of the examined cases. Smooth muscle myosin was widely distributed not only in the tumor cells of smooth muscle origin such as leiomyosarcoma and angioleiomyoma, but also in the tumor cells showing myofibroblastic differentiation such as malignant fibrous histiocytoma and in the epithelial components of synovial sarcoma. The results showed that skeletal muscle myosin can be regarded as an excellent marker in the diagnosis of rhabdomyosarcoma and that smooth muscle myosin is a useful marker of leiomyosarcoma and leiomyomas, and of tumors with myofibroblastic differentiation.

Adolescent↗
PubMed1985

Nuclear changes in colo-rectal epithelium with special reference to nuclear inclusions in carcinoma, dysplasia, adenoma and Peutz-Jeghers polyps.

The incidence and types of unusual nuclear structures (UNS) were examined based on the observation of randomly photographed 1,919 nuclei in total from the normal epithelium, dysplasia, Peutz-Jeghers type polyp, adenoma and carcinoma of the large bowel. These nuclear structures were classified as filamentous, granular and vesicular inclusions, and invaginated structures were also taken into consideration. Although all types of UNS were found in the normal epithelium, carcinoma cells had the most numerous UNS, especially of the invaginated type. The possible process of nuclear inclusion (NI) formation was discussed in connection with malignant transformation of colo-rectal epithelial cells.

Adenoma↗
PubMed1984

Immunohistochemical and ultrastructural demonstration of keratin in epi-myoepithelial islands of autoimmune sialadenitis in man.

Immunohistochemistry of salivary gland suggested that keratin is a specific marker of duct-epithelial cells and myosin for myoepithelial cells. Epi-myoepithelial islands found in some autoimmune sialadenitis, such as Sjögren's syndrome, were mainly composed of keratin-positive cells. Keratin filaments, with bundles and desmosome-attachments were invariably found in epithelial cells with electron microscopy. The islands contained no cells with myoepithelial characteristics. The findings show that there is no obvious participation of myoepithelial cells in the growth of the epi-myoepithelial islands.

Cytoskeleton↗
PubMed1984

Antibody against 25,000 dalton tryptic fragment of subfragment-1 from chicken skeletal muscle myosin: functional implication of the 25,000 fragment region in subfragment-1.

Antibody was prepared against the 25,000-dalton tryptic fragment of subfragment-1 from skeletal muscle myosin. The antibody was found to inhibit the Mg2+-ATPase activity and the initial P1-burst of the ATPase. The antibody suppressed the ATP-induced fluorescence enhancement of S-1, though it did not suppress the binding of ATP to S-1. The acto-S-1 ATPase activity was also inhibited by the antibody. These results suggest that there is a site in the 25K fragment region responsible for the transition of the myosin-ATP complex to another high energy complex.

Adenosine Triphosphatases↗
PubMed1984

A comparative study on the immunolocalization of keratin and myosin in salivary gland tumors.

Surgical specimens of the salivary gland tumor were studied by immunohistochemical techniques using the anti-keratin antibody and the anti-myosin antibody. In the normal tissue, keratin was localized predominantly in the duct epithelial cells and myosin in the myoepithelial cells. According to the immunohistochemical staining patterns, the tumors were able to be divided into two groups: one group consisted of pleomorphic adenoma, adenoid cystic carcinoma, and adenocarcinoma which showed a mixture of keratin- and myosin-positive cells, respectively, mimicking the structures of the intercalated duct; the other comprised monomorphic adenoma and mucoepidermoid tumor which disclosed keratin-positive cells predominantly, resembling the constituent of the excretory duct. These results were mostly consistent with the "bicellular theory" that the salivary tumors generate from the intercalated duct reserve cells and the excretory duct reserve cells.

Adenocarcinoma↗
PubMed1984

[Immunohistochemical localization of cytoskeletal proteins and thyroglobulin in thyroid micro cancers].

We performed a comparative study using immunoperoxidase staining on 11 cases of thyroid micro cancer (TCM) and 7 cases of clinically manifested cancers (CMC). Antibodies against 4 kinds of cytoskeletal proteins and thyroglobulin were used. In the TCM and CMC groups, actin and myosin were identified in almost all neoplastic cells of all patients; keratin and vimentin were present in the tumor cells of several patients. Keratin was found only in papillary carcinoma cells. Thyroglobulin was present in the neoplastic cells of several patients from both groups; follicular carcinoma cells and keratin-negative cells reacted more strongly with thyroglobulin than papillary carcinoma cells or keratin-positive cells. There was no special difference between TMC and CMC in the localization of cytoskeletal proteins and thyroglobulin.

Adenoma↗
PubMed1984

[Immuno-cytochemical and -histochemical localization of human keratin proteins in various kinds of cancerous lesion].

Immunoperoxidase staining for human keratin proteins (hKP) was performed cytochemically in samples from 79 cancer patients, and histochemically in samples from 134 cancer patients. Immunohistochemically, hKP was present in almost all patients with squamous cell carcinoma (lung), transitional cell carcinoma (urinary bladder), adenocarcinoma (lung, stomach, breast, ovary), bronchiole-alveolar carcinoma (lung), and large cell carcinoma (lung). It was detected in 40% of the patients with small cell carcinoma (lung). Histochemically, hKP was present in patients with squamous cell carcinoma (lung, uterine body), adenocarcinoma (lung, stomach, colon, gall bladder, thyroid, uterine body), adenosquamous cell carcinoma (gall bladder, uterine body), Signet-ring cell carcinoma (stomach), clear cell carcinoma (uterine body) and undifferentiated carcinoma (uterine body). However, it was not detected in patients with brochiole ++-alveola ++ carcinoma (lung) and mucinous carcinoma (gall bladder).

Breast Neoplasms↗
PubMed1983

[Oral amelanotic melanoma--report of a case with desmoplastic changes at the site of lymph node metastasis].

Amelanotic melanoma of the gingiva in a 59-year-old Japanese woman is presented. The histologic diagnosis of melanoma was confirmed by the concurrent lentigo maligna in the palatal mucosa and desmoplastic malignant melanoma (DMM) in the metastatic foci of a cervical lymph node. Electron-microscopical observations revealed that DMM cells exhibited mesenchymal metaplasia or myofibroblastic differentiation. Accordingly, collagen synthesis of the tumor cells was suspected. A review of 31 reported DMM cases is also presented.

Female↗