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At least 19 recordsLinked to original sources
PubMed1988

Sea urchin morphogenesis and cell-hyalin adhesion are perturbed by a monoclonal antibody specific for hyalin.

We have generated and characterized a monoclonal antibody (McA Tg-HYL) that recognizes sea urchin hyalin as evidenced by immunofluorescence staining of the hyaline layer (HL) and immunoblot staining of the hyalin protein band. On immunoblots of HL extracts only the hyalin protein reacted with McA Tg-HYL. Immunoprecipitates of radioactive proteins from embryos incubated with [35S]methionine yielded radioactive hyalin and 190, 140 and 105 x 10(3) Mr proteins associated with hyalin. McA Tg-HYL was generated against Tripneustes gratilla embryos but reacts with hyalin from the distantly related sea urchin species, Colobocentrotus atratus, Strongylocentrotus purpuratus, Arbacia punctulata, Lytechinus variegatus and Lytechinus pictus. Developing embryos of the above-mentioned six species were treated with McA Tg-HYL and did not gastrulate or form arms. Observations of treated embryos revealed areas of separation of the hyaline layer from the underlying embryonic cells, suggesting that McA Tg-HYL was interfering with binding of the cells to the HL. Using the centrifugation-based adhesion assay of McClay et al. (Proc. natn. Acad. Sci. U.S.A. 78, 4975-4979, 1981), Fab' fragments of McA Tg-HYL were found to inhibit cell-hyalin binding. McA Tg-HYL did not inhibit hyalin gelation in vitro or the reaggregation of dissociated blastula cells. We postulate that McA Tg-HYL recognizes an evolutionarily conserved hyalin domain involved in cell-hyalin binding and required for normal epithelial folding.

Animals↗
PubMed1988

Roles for Ca2+, Mg2+ and NaCl in modulating the self-association reaction of hyalin, a major protein component of the sea-urchin extraembryonic hyaline layer.

The self-association reaction of hyalin, a major protein component of the sea-urchin extraembryonic hyaline layer, was examined. Concentrations of Ca2+ below 1 mM had little effect on the hyalin gelation reaction, but higher concentrations of the cation induced protein aggregation. Quantitative aggregate formation required a Ca2+ concentration in excess of 10 mM. This reaction was modulated by both NaCl and Mg2+. The effectiveness of Ca2+ in inducing hyalin gelation was markedly enhanced in the presence of 500 mM-NaCl, the concentration found in sea water. Similarly, 20 mM-Mg2+ also enhanced Ca2+-induced hyalin gelation. Neither NaCl nor Mg2+ alone induced hyalin gelation. Concentrations of Ca2+ as low as 1 mM effectively protected hyalin from tryptic digestion both in the presence and in the absence of 500 mM-NaCl. The latter result suggested that, although higher concentrations of Ca2+ were required to induce the hyalin gelation reaction, lower concentrations of the cation could mediate a protein-protein interaction in an NaCl-independent fashion. These results identify the parameters that modulate hyalin self-association, a reaction that is essential for hyaline-layer assembly around the developing sea-urchin embryo.

Animals↗
PubMed1986

Pulmonary cytoplasmic hyalin resembling Mallory's alcoholic hyalin in the liver.

Sixty-three consecutive autopsy cases of interstitial fibrosis of the lung, 6 cases of organizing pneumonia, 14 of pneumocystis pneumonia, and 20 of acute bacterial pneumonia complicating as a terminal illness listed in our Department of Pathology during a period from 1978 to 1983 were surveyed for Mallory body-like cytoplasmic hyalins in the alveolar cells. We found the hyalins in 10 of 63 cases (15.9%) with interstitial fibrosis of the lung and one of 6 cases with organizing pneumonia. Seven of the former 10 had an associated malignancy; 3 esophageal cancers, 2 lung cancers, and 2 leukemias. Five of the seven patients received an irradiation for treatment of their malignancies, subsequently developed interstitial fibrosis of the lung. Among the remaining 3 of the 10, one showed diffuse interstitial fibrosis associated with rheumatoid arthritis and two had an idiopathic type of diffuse pulmonary fibrosis. There was only one case in which the pulmonary hyalins were found in the absence of extensive interstitial fibrosis within small organizing foci of peribronchial and subpleural location. Pulmonary hyalins showed the same conventional staining properties and ultrastructural features as Mallory's alcoholic hyalins found in the liver, but did not reveal a simultaneous association with the hepatic hyalins. Pulmonary hyalins frequently stained positively with monoclonal anti-cytokeratin antibodies, more strongly at their periphery. Pulmonary hyalins were considered to be a non-specific reaction of alveolar cells to injuries, mostly in association with the pulmonary fibrosis of any etiology but not the hepatic hyalins.

Adult↗
PubMed1992

Hyalin, a sea urchin extraembryonic matrix protein: relationship between calcium binding and hyalin gelation.

The protein hyalin, a major component of the sea urchin extraembryonic hyaline layer, was previously shown to undergo a Ca(2+)-induced self-association into large aggregates (gelation). This reaction represented a major step in assembly of the layer. In the experiments reported here, digestion with trypsin resulted in a rapid dissociation of hyalin into a mixture of peptides which retained the capacity to bind Ca2+. However, unlike intact hyalin, none of these peptides associated into large aggregates (gelation) in the presence of Ca2+, Mg2+, and NaCl. Loss of the ability to undergo gelation was not accompanied by any significant change in the content of acidic plus amide amino acid residues. Decreasing the pH to 5.6 resulted in a loss of 25% of hyalin's Ca(2+)-binding capacity but had no effect on the ability of the protein to undergo gelation. Peptide fragments were only partially effective at inhibiting hyalin gelation. Clearly, not all the Ca(2+)-binding sites were required for hyalin gelation and Ca2+ binding alone was insufficient to drive this reaction. In addition, hyalin appeared to possess two classes of protein-protein interaction domains, one of which was essential for gelation.

Amino Acids↗
PubMed1988

Role of calcium in stabilizing the structure of hyalin, a major protein component of the sea urchin extraembryonic hyaline layer.

The interactions of NaCl and CaCl2 with the sea urchin embryo coat protein hyalin were investigated. Endogenous protein tryptophan fluorescence was enhanced by almost 45% in the presence of 200mM NaCl while 1mM CaCl2 reversed this effect and brought the intensity of fluorescence back close to that of the native protein. Half-maximal concentrations of 53 and 0.32mM were determined for NaCl and Ca+2, respectively. Hyalin conformation, as measured by circular dichroic spectroscopy, was altered by NaCl and CaCl2 in a fashion parallel to the effects of these salts on tryptophan fluorescence. Sodium chloride disrupted hyalin secondary structure while CaCl2 affected the return of hyalin to its native conformation. The interactions of NaCl and CaCl2 with hyalin were not modulated by MgCl2. These results suggest a role for CaCl2 in stabilizing hyalin against the disruptive effects of the high concentration of NaCl present in sea water.

Animals↗
PubMed1991

Assembly of the sea urchin extraembryonic hyaline layer; Ca2+ and Mg2+ act independently and at different sites on the pathway leading to hyalin-gel formation.

We have studied the interactions of Ca2+ with the sea urchin extraembryonic coat protein hyalin. As reported previously, Ca2+ alone was ineffective in inducing hyalin-gel (large aggregate) formation. This reaction required the additional presence of Mg2+ and NaCl. However, the results of tryptic digestion and nondenaturing agarose gel electrophoresis experiments demonstrated that Ca2+ could induce hyalin self-association into small aggregates in the absence of Mg2+ and NaCl. Magnesium did not modulate the interactions of Ca2+ with hyalin. In addition, Mg2+ had minimal effects on the conformation of hyalin. These results have been incorporated into a model delineating the pathway leading to hyalin-gel formation.

Animals↗
PubMed1986

Cytoplasmic hyalins resembling Mallory's alcoholic hyalins in pulmonary carcinoma cells.

Two cases with Mallory body (MB)-like cytoplasmic hyalins in cells, which were quite uncommon as MB-having cells, were presented. The cases were 61-and 59-year-old males. MB-like hyalins were found in large cell carcinoma cells of giant cell type of the lung. The cells containing MB-like hyalins frequently showed a hydropic swelling of the cytoplasm with pyknotic, or wrinkled nuclei. Histochemical properties of the hyalins were just similar to those of hepatic MBs in alcoholic liver diseases. Electromicroscopically, the hyalins were composed of granular, or homogeneous electron dense materials with the peripheral meshwork of randomly oriented fibrils measuring about 100A in diameter. These were stained with anticytokeratin antibodies, suggesting the relateness of the hyalins to intermediate-sized filaments of the cytokeratin type.

Carcinoma↗
PubMed1970

Some properties of hyalin: the calcium-insoluble protein of the hyaline layer of the sea urchin egg.

The principal protein component of the hyaline layer of sea urchin eggs is the calcium-insoluble protein first described by Kane and Hersh. The protein hyalin is abnormally high in acidic amino acids, almost devoid of basic amino acids, and characteristically rich in valine and proline. Essentially all of the cysteine present is found in the disulfide form; no evidence points to intermolecular disulfide linkages. Hyalin from several species has a minimal subunit weight of about 100,000, though evidence exists for a particle three times this weight in urea or guanidine hydrochloride from one species. Optical rotatory dispersion measurements indicate no alpha-helix content, though the dispersion has unique characteristic features. Addition of small quantities of calcium causes hyalin to gel to a birefringent fibrous form. The fibrous, birefringent form of hyalin is rendered isotropic upon addition of EDTA, but the birefringence is restored with re-addition of divalent cation.

Animals↗
PubMed1979

Systemic hyalinosis (juvenile hyaline fibromatosis). Ultrastructure of the hyaline with particular reference to the cross-banded structure.

Systematic hyalinosis (juvenile hyaline fibromatosis) is characterized by hyalinized skin lesions. Electron microscopic examination of a hyalinized skin tumor from a 19-year-old man with this syndrome revealed that the hyaline was composed of ruthenium red-positive ultrastructures (granules, filaments, and a kind of cross-banded structure), indicating the presence of glycosamino-glycan or glycoprotein, and a small number of thin collagen fibrils. Using a new ruthenium red staining method combined with an enzymatic digestion procedure, it was demonstrated that the cross-banded structure and granules consisted of chondroitin sulfate-proteoglycan and/or glycoprotein, and that the cross-banded structure is probably a noncollageneous aggregate of the granules attached to the parallel-arranged filaments of hyaluronic acid-like nature.

Adult↗
PubMed1980

An unusual degenerative disorder of neurons associated with a novel intranuclear hyaline inclusion (neuronal intranuclear hyaline inclusion disease). A clinicopathological study of a case.

A 21-year-old woman with an unusual, progressive, degenerative neurological disorder is described. The disorder is characterized clinically by behavioral abnormality, peculiar involuntary movements, and ataxia starting in early childhood and subsequent development of dementia, choreoathetosis, rectal and bladder incontinence, bulbar and spinal muscular weakness, pes cavus, kyphoscoliosis, and generalized seizures. The clinical manifestations are correlated, with widespread pathological changes affecting almost all neuronal systems. The pathological changes are discussed in relation to the wide spectrum of "multisystem atrophies." Particular attention is directed to the ubiquitous occurrence of a novel intranuclear, eosinophilic, hyaline inclusion in almost all types of central, peripheral, and autonomic neurons. The ubiquitous neuronal involvement seems to explain the diffuse multiple system degeneration. The pathogenesis of the neuronal inclusions is unknown, but it is speculated that the disorder may represent a metabolic abnormality affecting the nuclear protein of neurons, rather than a viral infection. The pathological features, consisting of the neuronal intranuclear hyaline inclusions associated with multiple system atrophy, have not hitherto been described, and "neuronal intranuclear hyaline inclusion disease" is proposed as a name for the disorder. Rectal biopsy demonstrating the intranuclear hyaline inclusions in ganglion cells of the hyenteric plexuses may serve as a diagnostic procedure for the disorder.

Adult↗
PubMed1975

Hepatocellar hyalin (Mallory bodies) in long term griseofulvin-treated mice: a new experimental model for the study of hyalin formation.

Experimental studies on the significance and origin of hepatocellular "alcoholic" hyalin (Mallory bodies) are hampered by the lack of a suitable animal model. In the present paper, the experimental production of hepatocellular hyalin identical with human alcoholic hyalin both light and electron microscopically in long term griseofulvin-treated mice is described. Moreover, the results conclusively disprove the specificity of Mallory alcoholic hyalin for alcohol-induced liver cell damage.

Alcoholism↗