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Y Matuo

Publications and source records attributed to Y Matuo.

At least 37 records · Page 2Linked to original sources
PubMed1988

Comparative analysis of growth factors in normal and pathologic human prostates.

Growth factors, as detected by DNA synthesis stimulating activity for BALB/c 3T3 cells, in normal, benign hypertrophic and cancerous human prostates were analyzed. The total content (units per gram of tissue) in benign hypertrophic prostate was two to four times higher than those in normal and cancerous prostates. In all the three groups, heparin-binding growth factor, growth factor adsorbed to heparin-Sepharose in the presence of 0.5 NaCl. accounted for about 80-95% of the total growth factor content. Qualitative analysis using a heparin-Sepharose column revealed two types of heparin-binding growth factor in the prostates, one eluted from the column at 1.2-1.3 M NaCl and the other at 1.5-1.8 M NaCl. The latter was the predominant type in all groups. In addition to the growth factors detected with BALB/c 3T3, a growth factor with specific action upon MC3T3-E1 mouse osteoblasts was found in prostatic cancer, but not in normal and benign hypertrophic prostates.

Animals↗
PubMed1988

Partial purification of a major type of rat prostatic growth factor: characterization as an epidermal growth factor-related mitogen.

The dorsolateral prostate of rats contains a mitogen that shares several properties with epidermal growth factor (EGF), which was designated as prostatic EGF-related mitogen (PEM). PEM was purified about 2,100-fold using molecular-sieve and ion-exchange chromatography. Final preparation stimulated DNA synthesis in BALB/c 3T3 cells at a concentration as low as 1.5 ng/ml and competed with 125I-EGF for binding to cell surface receptors. PEM had a molecular weight of about 14,000 and an isoelectric point of about 4.5, being heat- and acid-stable but inactivated by dithiothreitol. The primary cultured rat dorsolateral prostate epithelial cells required EGF for maximum growth. Partially purified PEM fully substituted for EGF in the primary culture system at a concentration as low as 90 ng/ml. However, the activity of PEM was hardly suppressed by antimouse EGF antiserum. These findings suggest that PEM is a member of the EGF family but has a higher molecular weight (high molecular weight EGF).

Animals↗
PubMed1988

Production of IGF-II-related peptide by an anaplastic cell line (AT-3) established from the Dunning prostatic carcinoma of rats.

AT-3 cells, one of anaplastic cell lines established from the Dunning prostatic carcinoma of rats, were able to grow under serum-free conditions in a state of suspension detached from a substratum. Radioimmunoassay using monoclonal antibody against rat insulin-like growth factor II (IGF-II) revealed the presence of IGF-II-related peptide in acid-ethanol extracts of lyophilized serum-free media conditioned by AT-3 cells. The peptide contents in the culture media increased with increase in cell number; 71 ng at 3.0 X 10(6) cells and 449 ng at 4.6 X 10(7) cells. IGF-II-related peptide was hardly detectable in acid-ethanol extracts of AT-3 cells harvested after 13-days culture. These results indicate that AT-3 cells produce IGF-II-related peptide and may release it into the culture media.

Animals↗
PubMed1988

Proliferation of epithelial cells derived from rat dorsolateral prostate in serum-free primary cell culture and their response to androgen.

Primary cultured epithelial cells derived from the rat dorsolateral prostate proliferated in serum-free nutrient medium WAJC 404 supplemented with mitogens: insulin (650 nM), cholera toxin (120 pM), epidermal growth factor (EGF) (2.5 nM), dexamethasone (300 nM), and bovine pituitary extract (25 micrograms/ml). The culture consisted of two types of epithelial cell colonies: one originated from single cells or small cell aggregates and the other was epithelial cell outgrowth from small tissue fragments attached to a substratum. There were differences in requirements for the mitogens between the two types of colonies. Requirements for cholera toxin, bovine pituitary extract, and dexamethasone were higher in the former type of colonies, and those for EGF were higher in the latter type of colonies. Proliferation of the epithelial cells in either type of colony was suppressed more than 50% by 1 nM dihydrotestosterone. This suppressive effect was not mediated by stromal component in the tissue fragments, and was counteracted by cyproterone acetate, indicating specific and direct action of the androgen on prostate epithelial cells. The results suggest that there is discrete participation of polypeptide growth factors and androgen in proliferation and differentiation, respectively, of prostate epithelial cells in vivo.

Androgens↗
PubMed1988

Stabilization of fibroblast growth factors by a non-cytotoxic zwitterionic detergent, 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate (CHAPS).

The potential usefulness of a zwitterionic detergent, 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate (CHPAS), in the stabilization of acidic and basic fibroblast growth factors (FGFs) was examined. Among several detergents, CHAPS was found to be not only non-cytotoxic but also most useful in handling the diluted preparations of FGFs. The advantages are as follows: 1) at lower concentrations than 0.01% CHAPS did not affect growth factor activity of calf serum (CS) and the growth rate of BALB/c 3T3 cells. The primary culture of rat prostate epithelium and colony formation of NRK-49F cells were hardly influenced by CHAPS lower than 0.003%; 2) the loss of FGFs that usually occurs due to their adherence to the surface of storage containers was effectively prevented by inclusion of 0.1% CHAPS; 3) the recovery of FGFs after storage or dialysis was significantly enhanced by inclusion of 0.1% CHAPS; 4) CHAPS at lower concentrations than 0.1% does not interfere with amino acid analysis, except that Thr may be misled only when the ratio of protein/CHAPS is low; 5) amino acid sequence analysis was hardly disturbed by CHAPS up to 0.5%. These results indicate that CHAPS is useful as a stabilizing agent for various kinds of polypeptides capable of showing biological activity at a low concentration.

Amino Acids↗
PubMed1988

[A case of leiomyoma of the spermatic cord].

A 46-year-old man visited our clinic with the chief complaint of indolent swelling of the left scrotal contents. An elastic hard and fist-sized mass with negative transillumination was palpable in left scrotum, but testis and epididymis were not discriminated. Left high orchiectomy was performed. Tumor was 90 X 55 mm in size and the testis and epididymis at the lower pole of the tumor were intact. Histological diagnosis was leiomyoma and we diagnosed leiomyoma of the spermatic cord. To our knowledge, this is the 5th case reported in Japan.

Genital Neoplasms, Male↗
PubMed1987

Heparin binding affinity of rat prostatic growth factor in normal and cancerous prostates: partial purification and characterization of rat prostatic growth factor in the Dunning tumor.

The rat prostate contains two types of growth factors capable of stimulating DNA synthesis in BALB/3T3 cells. These rat prostatic growth factors (RPGF) were separable by a different affinity for heparin: low affinity type RPGF and high affinity (HiA) type RPGF. About 80% of the RPGF in the cytosol from normal prostates was low affinity type, whereas more than 80% in the cytosol from the Dunning tumors was HiA type. Elution profile of HiA-RPGF showed two peaks of activity eluted from the heparin-Sepharose column, one at 1.3-1.4 M NaCl (HiA1-RPGF) and the other at 1.6-1.7 M NaCl (HiA2-RPGF). HiA2-RPGF could be purified 1100-fold from the Dunning tumor (AT-3 subline) in about 20% recovery by heparin-Sepharose chromatography. The partially purified HiA2-RPGF in the Dunning tumor has a molecular weight of about 19,000 and isoelectric point of about 3.8, and stimulated DNA synthesis at a concentration of about 0.25 nM. The activity was lost by heat treatment at 70 degrees C for 5 min and by acid treatment, whereas it was stimulated by incubating with dithiothreitol. The HiA2-RPGF did not have transforming growth factor activity at a concentration of 250 ng/ml or lower in the presence of epidermal growth factor.

Animals↗
PubMed1987

Isolation of a 41 kilodalton cytosol protein from the Dunning rat prostatic adenocarcinoma: characterization as depolymerized actin isomers.

Except for albumin, a 41,000-dalton protein (41K) in the cytosol of the Dunning R-3327 rat prostatic adenocarcinoma was found to be the most abundant soluble protein. This protein was purified in nearly homogeneous state by conventional chromatographies. After the first chromatography, because of the adhesive nature of the protein, 0.5% SDS and 2 M urea were necessary for subsequent steps of purification. The amino acid composition of the purified 41K was similar to that of actin isolated from rabbit skeletal muscle. Alternatively, 41K could be extracted from the Dunning tumor in the presence of ATP and dithiothreitol, under conditions in which actin molecules are depolymerized, and could be purified by the same method as cytoskeletal actin. The purified protein showed properties similar to rat skeletal muscle actin in amino acid composition and antigenicity. Both 41K proteins were found to be composed of four components having different isoelectric points. These results indicate that most actin exists in a depolymerized form as a cytosol protein of 41,000 daltons in the Dunning tumor and is composed of at least four isomers.

Actins↗
PubMed1987

Protein profiles of benign hypertrophic prostate: stroma-abundant distribution of BPH-associated nonhistone proteins.

Mechanically isolated epithelium and stroma from benign hypertrophic prostates were highly pure on the basis of histochemical and biochemical criteria. By electrophoretic analyses, whole cellular and nuclear proteins were compared among whole tissues, epithelium, and stroma. The characteristic protein profiles of benign hypertrophic prostates were reflected in the electrophoretic patterns of the stroma. Two-dimensional gel electrophoretic patterns of the epithelium were different from those of the stroma with exception of about 18 major spots that were common to both fractions. Of the protein species separated, 35K/6.7 (molecular weight/pI) and 36K, which was composed of two species with pI of 4.4 and 4.6, were abundant in the epithelium and stroma, respectively. Nuclei prepared from whole tissues of benign hypertrophic prostates contained three kinds of nonhistone proteins (NHP) closely associated with benign prostatic hypertrophy (BPH); 42 K-NHP, 55 K-NHP and 190 K-NHP. Electrophoretic analysis of the nuclear proteins revealed that all the BPH-associated nonhistone proteins were abundantly distributed in the nuclei of the stroma.

DNA↗
PubMed1987

Growth factors in the prostate.

Certain local tissue factors, such as growth factor, in addition to androgens, are involved in the prostate growth. The prostate contains two types of growth factors capable of stimulating DNA synthesis in BALB/3T3 cells. They were divided into low affinity (LoA) type and high affinity (HiA) type by a different affinity for heparin-Sepharose. HiA-type growth factor is further classified into acidic HiA and basic HiA types. Acidic HiA type could be purified from the Dunning tumor (R 3327), a rat prostatic adenocarcinoma, and has a molecular weight of about 19,000 and a pI of about 3.8. Basic HiA type could be isolated from the tissues of human benign prostatic hypertrophy and has a molecular weight of about 12,000 and a pI of about 10.5. They are inactivated by heat and acid treatments. Acidic HiA type appears to be involved in growth of the rat prostate epithelium, and LoA type growth factor is possibly relevant to reproductive physiology because of its coexistence with "probasin," a major secretory protein in the dorsolateral prostate having a strong affinity for spermatozoa.

Aging↗
PubMed1986

Lobe-specific distribution of a 20,000-dalton nonhistone protein in the dorsolateral prostate of rats.

Distribution of an androgen-dependent, 20,000-dalton nonhistone protein with a pI of about 11.5 (20K-NHP) was examined by electrophoretic techniques. Nuclei of the brain, liver, spleen, skeletal muscle, lung, and thymus of rats contained a negligible amount of 20K-NHP, whereas 20K-NHP was distinctly detectable, in different relative amounts, in the nuclei of the male accessory sex organs, with the dorsolateral prostate having the highest relative content (100%), followed by the coagulating gland (approximately equal to 16%), the ventral prostate (approximately equal to 6%), and the seminal vesicle (approximately equal to 2%). There were heterogeneous distributions of cytosol components, acid phosphatase isozymes, and nonhistone proteins in the dorsolateral prostate. Zinc was localized in the lateral lobe, and fructose and glucose were in the dorsal lobe. Cytosol proteins with pI 7.5, 8.2, and 8.5 were abundant in the dorsal lobe, and proteins with pI 7.4 and 8.0 in the lateral lobe. Acid phosphatase isozymes with pI 7.1, 7.4, 7.7, and 8.0 were abundantly distributed in the lateral lobe. Of the nonhistone proteins, 20K-NHP showed the highest content both in the lateral lobe and in the dorsal lobe. It was found that 20K-NHP was more abundantly distributed in the lateral lobe (maximally four times higher) than in the dorsal lobe. The heterogeneous distribution of 20K-NHP in the dorsolateral prostate was strikingly similar to that of zinc. It appears, therefore, that 20K-NHP is closely related to dorsolateral prostate zinc content.

Acid Phosphatase↗
PubMed1985

A human prostatic growth factor (hPGF): partial purification and characterization.

A growth factor capable of stimulating DNA synthesis of BALB/3T3 cells was purified about 1,000-fold from the cytosol of human benign hypertrophic prostates by heparin-Sepharose chromatography; the growth factor bound to the column in the presence of 0.5 M NaCl was eluted with 1.5-1.7 M NaCl. Its molecular weight and isoelectric point were estimated to be 11,000-13,000 and 10.5, respectively. It was sensitive to heat- and acid-treatments but resistant to disulfide-reducing agent. The final preparation was able to stimulate DNA synthesis at 10 ng/ml. The degree of stimulation was dependent on serum concentration in the assay system; the degree of maximum stimulation increased about 5 times as serum concentration increased from 0.2 to 2%.

Cytosol↗
PubMed1985

Quantitative solubilization of nonhistone chromosomal proteins without denaturation using zwitterionic detergents.

Of three kinds of commercial zwitterionic detergents [SB 12, SB 14, and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (Chaps)], SB 12 and Chaps were more useful than SB 14 because of high solubility and less interference with protein assay. Efficiency for protein solubilization at pH 6-9 was higher for SB 12 than for Chaps with either calf thymus chromatin or rat liver nuclei. At pH 9 and ionic strength (I) = 0.35, 1% SB 12 and 1% Chaps were capable of solubilizing about 70% and about 47% of total proteins in rat liver nuclei, respectively. Core histones in rat liver nuclei were extracted to a lesser extent with Chaps than with SB 12. DNA-dependent RNA polymerase and isopeptidase activities were barely inactivated by 1% Chaps at pH 8-9, but isopeptidase activity was inhibited by 0.3% SB 12. These facts indicate that whereas SB 12 is effective for solubilization of whole nuclear proteins, Chaps is suitable for the selective extraction of nonhistone chromosomal proteins without denaturation.

Animals↗
PubMed1985

Localization of prostatic basic protein ("probasin") in the rat prostates by use of monoclonal antibody.

Isolated nuclei of the rat prostates contain a unique androgen-dependent basic protein, "probasin". Despite that it was hardly detectable in the cytosol centrifugally prepared from the prostates, immunofluorescent histological analysis of whole tissues using monoclonal antibody, which was raised against probasin purified from the nuclei, revealed that probasin was abundantly localized in the lumen and acinal regions of the epithelium, but hardly in the nuclei. Previous extraction of secretory fluid from the prostates caused about 60% decrease in the probasin content of isolated nuclei. These suggest that probasin was originally a secretory component in the prostates, being redistributed from the secretory fluid and granule into nuclei during fractionation of subcellular components.

Androgen-Binding Protein↗
PubMed1985

Differences in nonhistone protein changes in rat ventral and dorsolateral prostate during sexual maturation.

Age-related changes of chromosomal proteins in the dorsolateral and ventral prostates of rats from 6 to 31 weeks of age were studied by SDS-polyacrylamide gel electrophoresis. A nonhistone protein having a molecular weight of about 20,000 (20K-NHP), abundantly localized in the dorsolateral prostate, increased rapidly in content during the early stage of sexual maturation (6-11 weeks of age) in association with increases of serum testosterone concentration and prostatic tissue weight. Serum testosterone concentration decreased after week 11 and then remained constant until week 31. In contrast, the 20K-NHP content continued to increase after 11 weeks of age in the dorsolateral prostate, but not in the ventral prostate. The rapid increase of 20K-NHP in the dorsolateral prostate during the early stage of sexual maturation could not be attained in immature rats (5 weeks of age) by injection of excess amounts of androgens and/or prolactin for a week. But the 20K-NHP content in the ventral prostate of rats treated with testosterone propionate was almost the same as that of mature rats.

Androgens↗
PubMed1985

Comparison of subcellular proteins of normal prostate, benign prostatic hypertrophy, and prostatic cancer: presence of BPH-associated nonhistone proteins.

Proteins in the cytosol, postnuclear particulate, and nuclear fractions from seven specimens of normal prostate from bladder cancer patients, 14 specimens of benign hypertrophic prostate (BPH), and three specimens of cancerous prostate were analyzed and compared by SDS-polyacrylamide slab gel electrophoresis. Abundant protein species in the cytosol fractions were 60K (species having a molecular weight of about 60,000) and 42K; their relative contents were about 35% for 60K and about 12% for 42K. In the postnuclear particulate fraction, 42K was the most abundant (about 10% of the total). The contents of these major protein species were similar in specimens of normal and diseased prostates. In addition, there are marked similarities in the electrophoretic patterns for all the protein (24-29 species) in the cytosol and postnuclear particulate fractions of the human prostate, except for four minor species in the cytosol fraction. Of the nuclear proteins, the content of core histones (H2A, H2B, H3, and H4) was fundamentally similar among all the specimens, whereas the content of H1 histone was different from one specimen to another. The most remarkable and significant difference was that the 42K-NHP (nonhistone protein having a molecular weight of about 42,000), 55K-NHP, and 190K-NHP concentrations were significantly higher in BPH than in normal and cancerous prostates.

Chromosomal Proteins, Non-Histone↗
PubMed1984

Changes of an androgen-dependent nuclear protein during functional differentiation and by dedifferentiation of the dorsolateral prostate of rats.

Nuclei of the dorsolateral prostate of rats contain a large amount of androgen-dependent non-histone protein (20K-NHP) (mol. wt. not equal to 20,000; pI not equal to 11.5) (Matuo et al. (1]. Its content in the nuclei increased most markedly during 4-8 weeks of age, when functional differentiation of the prostate was most active on the basis of the changes of major cytosol proteins and zinc. Nuclei of the Dunning tumors originating in the dorsolateral prostate were found to lack 20K-NHP regardless of androgen dependency, indicating the disappearance of the 20K-NHP from the nuclei by dedifferentiation. These suggest that the 20K-NHP is an important nuclear protein for differentiation of the dorsolateral prostate cells.

Aging↗