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Biomedical subjects

L Raine

Publications and source records attributed to L Raine.

12 recordsLinked to original sources
PubMed1983

Lectin binding patterns in diffuse large cell lymphoma.

The staining reaction of a panel of lectins in paraffin embedded lymph node specimens of diffuse large cell lymphoma was studied in relation to survival. In 47 of 49 patients, varying degrees of lectin binding were observed with Ricinus communis agglutinin (RCA), crude extract of Arachis hypogaea (c-PNA), Concanavalin ensiformis A (Con A), Triticum vulgaris A (WGA) and Phaseolus vulgaris A (PHA). Binding was either absent or only minimal with Pisum sativum A (PSA) and Lens culinaris A (LCA). Two categories of binding were observed: cell surface and cytoplasmic. Cell surface binding was seen in tumor cells, while cytoplasmic binding was observed in macrophage-histiocytes. Varying numbers of tumor cells were stained with RCA, WGA, c-PNA or PHA; but with Con A virtually no tumor cells were stained. Stromal macrophage-histiocytes were stained with RCA, WGA, or Con A in all but one case, frequently with all three lectins; c-PNA binding macrophage-histiocytes were absent in one third of the cases. With PHA the staining of stromal macrophage-histiocytes was extremely rare. Tumor cells that stained with RCA but not with c-PNA were observed in 9 of 15 patients who survived more than 2 years after diagnosis. In all 15 long-term survivors, stromal macrophage-histiocytes were positive for c-PNA. Tumor cells that reacted with c-PNA but not with RCA were seen in five patients who survived less than two years. All 16 patients whose tumors lacked c-PNA binding stromal macrophage-histiocytes in the presence of RCA binding macrophage-histiocytes were short-term survivors. These observations suggest the heterogeneity of stromal macrophage-histiocytes as well as that of tumor cells. Furthermore, the variation of lectin binding might be useful in assessing prognosis.

Adolescent↗
PubMed1982

Warthin's tumor--epithelial cell differences.

An immunohistochemical technic to localize IgA and a histochemical technic to demonstrate beta-D-galactose and N-acetyl-S-galactosamine by peanut agglutinin are applied to paraffin-embedded sections of Warthin's tumor. The luminal layer of epithelium is positive for IgA, while the basal layer is positive for peanut agglutinin. The luminal layer epithelium apparently serves as the route through which IgA (derived from plasma cells in the lymphoid stroma) is secreted into the cystic spaces. The apical cytoplasmic staining for peanut agglutinin in the basal layer is uniquely different from the peanut agglutinin staining pattern in the normal parotid gland. We conclude that the two-layer epithelium of Warthin's tumor is different in morphology, biochemistry, and function.

Adenolymphoma↗
PubMed1982

Demonstration of myoglobin in formalin-fixed renal sections by immunoperoxidase technic.

The use of an immunohistochemical technic offers a very sensitive method to detect myoglobin in formalin-fixed, paraffin-embedded tissues. Thus, the technic is suitable for retrospective studies. Myoglobin can be demonstrated at the brush border and apical cytoplasm of the tubular epithelium of proximal tubules. Granular substances and casts in the lumens also react positively with antimyoglobin. Our findings confirm the results of a previous animal study, showing that myoglobin is filtered through glomeruli and reabsorbed by the proximal tubules.

Cytoplasm↗
PubMed1982

Discovery of a high affinity of Phaseolus vulgaris agglutinin (PHA) with gastrin-secreting cells.

A lectin, Phaseolus vulgaris agglutinin (PHA), isolated from the red kidney bean, was found to have a very high affinity with gastrin-secreting cells (G cells). The unique PHA-G cell interaction is confirmed by (1) G cell reaction only with PHA, not with other lectins, and (2) PHA reaction with G cells but not with other endocrine cells. The authors concluded that gastrin-secreting cells are composed of a large quantity of galactose-N-acetyl-glucose-manose-containing glycoconjugates. The significance of this glyco-conjugate in G cells is not ascertained. The use of a PHA histochemical technic may well be suitable to study the carbohydrate (or pathophysiological) changes in G cells.

Endocrine Glands↗
PubMed1982

Versatility of biotin-labeled lectins and avidin-biotin-peroxidase complex for localization of carbohydrate in tissue sections.

Carbohydrate residues in tissue can be localized by a very sensitive, specific, and simple technique, utilizing a biotin-labeled lectin followed by an avidin-biotin-peroxidase complex (ABC). Distribution of peanut receptors in benign and malignant tissues was found to be quite different. Normal colonic mucosa occasionally shows small dot staining in the supranuclear cytoplasm, while the tumor cells of colonic adenocarcinoma tend to show diffuse cytoplasmic or membranous staining. Normal breast ductal epithelium shows membranous staining at luminal borders, while medullary carcinoma of the breast shows distinct membranous and cytoplasmic staining. The use of this avidin-biotin-peroxidase complex technique may contribute to understanding the process of tumorigenesis as well as providing a sensitive method to determine early stages of malignant transformation.

Avidin↗
PubMed1981

Medullary carcinoma of breast: an immunohistochemical study of its lymphoid stroma.

Immunoperoxidase staining for IgA, IgG, IgM, and secretory component (SC) was performed on ten cases each of medullary carcinoma and infiltrating duct carcinoma of breast. Plasma cell-rich stroma of medullary carcinoma was found to contain predominantly IgA plasma cells. Tumor cells also contained IgA and SC. In contrast, the few plasma cells of infiltrating duct carcinoma were found to be predominantly IgG type, and the tumor cells contained none or very small amounts of IgA and SC. Because the presence of IgA plasma cells and IgA and SC in lining epithelial cells are characteristic features of organs of the secretory Ig system, these findings in medullary carcinoma may suggest a good degree of functional differentiation of these tumor cells and correlate well with the well-known favorable prognosis associated with this tumor.

Breast Neoplasms↗
PubMed1981

Spironolactone bodies. An immunoperoxidase study with biochemical correlation.

The present immunoperoxidase study attempted to localize aldosterone and cortisol in formalin-fixed paraffin-embedded adrenal glands or tumors. Apparently, steroid substances are solubilized during routine tissue processing, and the cytoplasm of adrenal cortical cells is not stained by either antialdosterone or anticortisol antibodies. However, spironolactone bodies react positively with antialdosterone antibody. The presence of aldosterone in the concentric laminations of spironolactone bodies supports the concept that spironolactone bodies are not artifacts. Furthermore, the fact that aldosterone does survive in spironolactone bodies suggests that it is bound in some unusual form. The spironolactone bodies are probably derived from endoplasmic reticulum, and the membranes of endoplasmic reticulum are considered capable of storing steroids. It is likely that during the formation of spironolactone bodies are probably derived from endoplasmic reticulum, and the membranes of endoplasmic reticulum are considered capable of storing steroids. It is likely that during the formation of spironolactone bodies, aldosterone or a few cortisol-like substances are trapped in these laminated concentric bodies.

Adrenal Glands↗
PubMed1981

A comparative study of the peroxidase-antiperoxidase method and an avidin-biotin complex method for studying polypeptide hormones with radioimmunoassay antibodies.

A highly sensitive immunoenzymatic technic is presented. The method involves three sequential steps: (1) primary antibody, (2) biotin-labeled secondary antibody, and (3) avidin-biotin-peroxidase complex. Avidin, an egg white protein, has four binding sites for the low-molecular-weight vitamin biotin. Many moieties of biotin can be coupled to the peroxidase molecule. Thus, since a relatively large amount of avidin is incubated with biotin-labeled peroxidase, avidin serves as a link between biotin-peroxidase molecules; in turn, biotin-peroxidase serves as a link between avidin molecules. Consequently, this large lattice-like complex with biotin-binding capability can be attracted to the sites of biotin-labeled antibody, producing a superior staining sensitivity. Several commercially available radioimmunoassay antibodies (e.g., antiglucagon, prolactin, gastrin, growth hormone, and thyroid-stimulating hormone antibodies) were tested for immunohistochemical staining. The unlabeled antibody peroxidase-antiperoxidase method fails to stain gastrin or thyroid-stimulating secretory cells when using these antibodies, and a relatively high antibody concentration is required to produce a positive reaction for glucagon, prolactin, and growth hormone. In contrast, the avidin-biotin-peroxidase complex method successfully demonstrates polypeptide hormones even when antibodies are diluted 20 to 40 times.

Antibodies↗
PubMed1981

The use of antiavidin antibody and avidin-biotin-peroxidase complex in immunoperoxidase technics.

Avidin has an extraordinary affinity for the small-molecule vitamin biotin. Covalently coupling biotin or avidin to peroxidase molecules does not interfere with their normal biochemical functions. The avidin or biotin molecules, either peroxidase conjugated or unconjugated, can be brought to the antigen sites by means of an antiavidin antibody. Several immunohistochemical staining technics based on this principal have been described. The method utilizing an avidin-biotin-peroxidase complex was found to be more sensitive than the unlabeled antibody (PAP) method. This method involved four sequential staining procedures: (1) primary antibody (goat anti-human antigen); (2) secondary antibody (rabbit antigoat IgG) added in relative excess; (3) goat antiavidin antibody; (4) avidin-biotin-peroxidase complex. The applications of this technic are discussed.

Animals↗
PubMed1981

Protein A, avidin, and biotin in immunohistochemistry.

Conjugated and unlabeled peroxidase antibody methods have proven to be quite satisfactory in localizing sites of antigen-antibody reaction. The use of avidin-biotin-peroxidase complex (ABC), as well as protein A, can contribute significantly to the field of immunohistochemistry. The sensitivity and specificity of several immunohistochemical methods is compared. In general, the ABC method produced the most intense staining and the least background staining of any method tested. The unlabeled antibody (peroxidase-antiperoxidase: PAP) method also yielded satisfactory results, but it was less intense than the ABC method. In comparison to the PAP method, the indirect conjugated method presented slightly inferior staining intensities and significantly higher background staining. Protein A techniques produced a range of staining sensitivities similar to or inferior to the PAP technique. The main disadvantage in using protein A is that it reacts with intrinsic immunoglobulin (Ig) G, thus producing an intense background. Therefore, its use is not recommended on tissues that have either abundant immunoglobulins in their interstitium or numerous IgG-containing plasma cells.

Avidin↗
PubMed1981

Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures.

The use of avidin-biotin interaction in immunoenzymatic techniques provides a simple and sensitive method to localize antigens in formalin-fixed tissues. Among the several staining procedures available, the ABC method, which involves an application of biotin-labeled secondary antibody followed by the addition of avidin-biotin-peroxidase complex, gives a superior result when compared to the unlabeled antibody method. The availability of biotin-binding sites in the complex is created by the incubation of a relative excess of avidin with biotin-labeled peroxidase. During formation of the complex, avidin acts as a bridge between biotin-labeled peroxidase molecules; and biotin-labeled peroxidase molecules, which contains several biotin moieties, serve as a link between the avidin molecules. Consequently, a "lattice" complex containing several peroxidase molecules is likely formed. Binding of this complex to the biotin moieties associated with secondary antibody results in a high staining intensity.

Avidin↗