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L A Sternberger

Publications and source records attributed to L A Sternberger.

At least 55 records · Page 3Linked to original sources
PubMed1980

Improved visualization of luteinizing hormone releasing hormone pathways by immunocytochemical staining of thick vibratome sections.

Using 100-micron thick Vibratome sections and a modification of the peroxidase--antiperoxidase method of immunocytochemical staining we achieve a Golgi-like image of luteinizing hormone releasing hormone (LHRH) cells and fibers in mouse brain. Five LHRH pathways are described: 1) A dense projection of fibers from LHRH cells in the medial preoptic and septal areas to the wall of the third ventricle; 2) a projection of fibers from neurons in the bed nucleus of the stria terminalis and the nucleus of the anterior commissure to the subfornical organ; 3) projections of fibers from neurons in the medial septal nucleus and the diagonal band of Broca to the olfactory bulb; 4) fibers which travel within or just lateral to the wall of the third ventricle from the organum vasculosum laminae terminalis to the median eminence; 5) cells and fibers located just dorsal to the optic tracts which project rostrally to the preoptic area and caudally to the level of the median eminence where they course medially to converge and enter the median eminence.

Animals↗
PubMed1979

Rich ependymal investment of luliberin (LHRH) fibers revealed immunocytochemically in an image like that from Golgi stain.

Immunospecific staining in 100-micron-thick Vibratome section by the unlabeled antibody method resembles Golgi staining and reveals an abundance of luliberin- (luteinizing hormone releasing hormone, LHRH) positive cells and fibers in close contact with the surface of the third ventricle. The polarity of LHRH cells can be seen and processes can be traced for several millimeters. In the medial preoptic and suprachiasmatic areas bipolar LHRH neurons send short stout processes to the ventricular surface and long processes toward the organum vasculosum laminae terminalis. These cells resemble the receptor cells contacting the cerebrospinal fluid that have been described by Vigh and Vigh-Teichmann [Vigh, B. & Vigh-Teichmann, I. (1973) Int. Rev. Cytol. 35, 189-251]. In the septal region some bipolar neurons send both of their processes towards the ventricular surface. LHRH neurons in the nucleus of the anterior commissure and the bed nucleus of the stria terminalis project over the anterior commissure to form a dense plexus of fibers in the subfornical organ. The proximity of LHRH perikarya and fibers to the ventricular surface supports the hypothesis [Knigge, K.M., Joseph, S.A., Scott, D.E. & Jacobs, J.J. (1971) in The Neuroendocrinology of Human Reproduction, eds. Mack, H.C. & Sherman, A.J., (Thomas, Springfield, IL), pp. 6-22.] that the cerebrospinal fluid functions in neuroendocrine control mechanisms.

Animals↗
PubMed1978

Estrogen receptor immunocytochemistry.

Estrogen receptor activity was preserved in fixed, paraffin-embedded tissue and demonstrated by binding of estrogen which, in turn, was detected immunocytochemically. Estrogen was added to rat endocervial epithelium to protect specifically receptors during fixation. The protective estrogen was apparently lost during embedding and had to be resupplied before staining. Estradiol-mediated immunocytochemical staining was inhibited by diethylstilbestrol and nafoxidine hydrochloride.

Animals↗
PubMed1978

Receptors for luteinizing hormone-releasing hormone.

Antisera to luteinizing hormone-releasing hormone (LH-RH) confer on Araldite sections of occasional rat pituitaries moderate immunocytochemical staining to the large secretory granules of gonadotrophs. Treatment of the sections with LH-RH before anti-LH-RH yields strong staining in all animals, irrespective of presence or absence of staining without pretreatment. This enhancement of staining is specific for LH-RH and is a high affinity, saturable reaction. Staining with or without LH-RH pretreatment is absent when anti-LH-RH absorbed with insolubilized LH-RH is used. Staining is inhibited by carboxyterminally-deficient LH-RH, unaffected by aminoterminally deficient LH-RH.

Adrenal Glands↗
PubMed1978

Adrenal luteinizing hormone releasing hormone receptors.

Paraffin sections of mouse adrenals processed with antiserum to luteinizing hormone-releasing hormone (LHRH) in the unlabeled antibody enzyme method reveal moderate staining in the cytoplasm of cells of zona fasciculata and reticularis. The stain is intensified upon pretreatment of sections with LHRH. Pretreated sections processed with solid phase immunoabsorbed LHRH are unstained. Analogues of LHRH deficient in the C-terminal glycine amide inhibit staining, while analogues deficient in the N-terminal pyroglutamic acid have no effect. It is concluded that the adrenal contains receptors for a ligand resembling LHRH in receptor and immunoreactivity. The possibility is considered that the ligand may be an inhibitor of pineal origin.

Adrenal Cortex↗
PubMed1978

Specificity of the immunocytochemical luteinizing hormone-releasing hormone receptor reaction.

Affinity-purified anti-LHRH, affinity-purified LHRH-anti-LHRH complex, as well as antisera depleted of anti-LHRH by solid phase immunoabsorption were used to test the specificity of the immunocytochemical approach for detection of receptor-bound LHRH. The solid phase immunoabsorbent was prepared by attaching LHRH to Sepharose via an RNase spacer. Purified anti-LHRH was eluted from the immunoabsorbent by acidification. Unabsorbed antisera as well as purified antibody conferred moderate immunocytochemical staining to the secretion granules of rat pituitary gonadotrophs. Staining intensity became greatly increased upon treatment of the electron microscopic sections with LHRH before immunocytochemical staining. All gonadotroph staining was abolished when absorbed antisera were used. The specificity of the immunoabsorbent was tested on mixtures of anti-LHRH and anti-ACTH17-39. On absorption of such mixtures with insolubilized LHRH, all gonadotroph staining disappeared, but the optical density indices of ACTH staining remained unaffected. It is concluded that gonadotroph secretion granules contain, in addition to an LHRH receptor reacting with LHRH in vitro, stable complexes of endogenous LHRH with receptor.

Adrenocorticotropic Hormone↗
PubMed1977

The unlabeled antibody enzyme method. Attempted use of peroxidase-conjugated antigen as the third layer in the technique.

The use of covalently bound peroxidase-immunoglobulin conjugate has been compared with soluble peroxidase-antiperoxidase complex as antigen in the third layer of the unlabeled antibody enzyme method. The conjugate conferred no staining. The low sensitivity of the conjugate appeared to be due in part to interference by unconjugated immunoglobulin and in part to diminution of antigenic reactivity of immunoglobulin as a result of conjugation. The triple specificity amplification inherent in the unlabeled antibody enzyme method with peroxidase-antiperoxidase complex may be lost if a peroxidase-immunoglobulin conjugate could be prepared in such a manner that staining occurs.

Animals↗
PubMed1975

Quantitative immunocytochemistry of pituitary receptors for luteinizing hormone-releasing hormone.

In Araldite sections of male rat pituitaries, stained after embedding by the unlabeled antibody enzyme method with antisera to native luteinizing hormone-releasing hormone (LH-RH) or LH-RH azo-conjugated to bovine serum albumin, localization is confined mainly to the interior of the large, and to a lesser extent to that of the small, secretion granules of the gonadotrophic cells. Plasma membranes are not demonstrated. Except for weak staining in the granules of corticotrophs, no other pituitary cell is stained. Pretreatment of sections with LH-RH (to dilutions of 4 pg/mul) increases staining intensity in the gonadotrophic granules. Other cells are unaffected. The lesser the gonadotroph staining intensity without pretreatment, the greater the increase (more than 23-fold reactivity). Augmented staining is measurable (P less than 0.001) to antiserum dilutions of 1:240000. Pretreatment with des-Glu-1-LH-RH, porcine corticotropin or rat prolactin has no effect. LH-RH-Gly-10(des-amide) inhibits. Rat glycoprotein hormones enhance staining with anti-azo-conjugated LH-RH. With antinative LH-RH these hormones enhance weak staining, but inhibit strong staining. Thick vibrotome sections of male rat or rabbit pituitaries stained before embedding reveal specific localization on plasma membrane and gonadotrophic secretion granules provided the sections have been pretreated with LH-RH (250 pg/mul). The data show that LH-RH after reaction with receptor is not sterically hindered from binding specific antibodies. Receptor may be found in secretion granules, both in the free state or combined with LH-RH. Plasma membrane receptor, on the other hand, was free under the conditions of the experiments. Immunization with LH-RH elicits not only heteroimmune antibodies specific for LH-RH, but also a group of still ill defined autoimmune antibodies, some of which may conceivably be reactive with glycoprotein hormone alpha-chains.

Absorption↗
PubMed1974

The role of cathepsin D in the pathogenesis of tuberculosis. A histochemical study employing unlabeled antibodies and the peroxidase-antiperoxidase complex.

Cathepsin D was visualized in free pulmonary alveolar macrophages (AM), in oil-induced peritoneal macrophages (MN) and in rabbit pulmonary and dermal BCG lesions with unlabeled antibodies and the peroxidase-antiperoxidase (PAP) complex. Large amounts of cathepsin D were present in AM and lower amounts in MN. In the lung this enzyme was richest in the alveolar macrophages that accumulated around the BCG lesions. In the dermal lesions, cathepsin D was in highest concentration in macrophages at the border of the necrotic (liquefying) centers. It was also found in high concentration in keratinizing cells of the dermal epithelium and hair follicles. It did not, however, increase appreciably in many of the activated macrophages that stained intensely for the lysosomal enzyme beta-galactosidase. In fact, many epithelioid cells with high beta-galactosidase activity contained no visible cathepsin D. This proteinase does not, therefore, seem to be primarily involved in the lymphocyte-mediated macrophage activation associated with acquired cellular resistance to tubercle bacilli. It is probably more involved with cell autolysis, with the digestion of ingested necrotic debris and, in all likelihood, with the process of liquefaction, the most adverse event in the pathogenesis of tuberculosis in man.

Animals↗