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Biomedical subjects

K Sanada

Publications and source records attributed to K Sanada.

At least 55 records · Page 3Linked to original sources
PubMed1987

Characterization and amino acid sequence of a new acidic cysteine proteinase inhibitor (cystatin SA) structurally closely related to cystatin S, from human whole saliva.

A cysteine proteinase inhibitor (designated as cystatin SA) was isolated from human whole saliva by procedures including chromatography on DE 32 and DEAE-Sepharose CL-6B. The amino acid sequence determined by conventional methods showed sequence homology of 90 and 87% as compared with the sequences of cystatin S and cystatin SN, respectively, both of which are salivary inhibitors characterized previously. The new inhibitor consisted of 117 residues and had a pI value of 4.3. Cystatin SA inhibited ficin and papain more strongly than cystatin S or cystatin SN did. It also exhibited inhibitory activity toward dipeptidyl peptidase I but the activity was much weaker than those toward ficin and papain.

Amino Acid Sequence↗
PubMed1986

Characterization of a new cysteine proteinase inhibitor of human saliva, cystatin SN, which is immunologically related to cystatin S.

A new cysteine proteinase inhibitor, cystatin SN, was purified from human whole saliva by chromatography with DE32, Sephacryl S200, and CM-Sepharose CL6B. Cystatin SN is immunologically related to cystatin S and both inhibitors have a similar molecular mass of about 13 kDa. The new inhibitor, however, was clearly distinguished from cystatin S by its much higher pI value. These inhibitors showed similar inhibitory activity for ficin, but cystatin SN was a much better inhibitor for papain and dipeptidyl peptidase I. The amino acid sequence of cystatin SN deduced in the light of the known structure of cystatin S indicates that they have 10 different amino acid residues in the sequence comprising in total 113 residues.

Amino Acid Sequence↗
PubMed1985

Inhibition of calcium-carbonate precipitation by human salivary proline-rich phosphoproteins.

The effects of the proline-rich phosphoproteins (PRP) on the rate of precipitation of CaCO3 from a CaCO3-supersaturated solution were examined by recording the absorbance at 570 nm and the pH, when 20 mM CaCl2 was added to 20 mM NaHCO3, in the presence or absence of proteins. The PRP suppressed CaCO3 nucleation and exhibited inhibitory effects on CaCO3 precipitation under those conditions and under stimulated physiological conditions (final concentration of Ca2+ was 2 mM and that of HCO-3 60 mM, pH was 8.0 at 37 degrees C). PRP may be of biological significance in maintaining homeostasis of the buffering system of saliva, which is mainly composed of bicarbonate, and in preventing the formation of stones consisting of CaCO3 in the salivary ducts.

Calcium Carbonate↗
PubMed1985

Intracellular localization of salivary peptide P-C-like immunoreactivity in the human pancreatic B-cells.

In order to clarify the intracellular localization of salivary peptide P-C-like immunoreactivity in human pancreatic B-cells, an immunohistochemical study at electron microscopic levels was carried out by the protein A-gold technique using antisera against insulin and salivary peptide P-C. Both salivary peptide P-C-like immunoreactivity and insulin-like immunoreactivity were present only in the insulin secretory granules of the pancreatic B-cells. However, the former immunoreactivity was lacking in many insulin secretory granules of foetal pancreatic B-cells while the latter immunoreactivity was seen in all insulin secretory granules. Salivary peptide P-C-like immunoreactivity was not found in the other kinds of cells in the islets. In a previous immunohistochemical study at light microscopic level, salivary peptide P-C-like immunoreactivity appeared in a few pancreatic B-cells at about the 16th week of gestation, in an increasing number during gestation, and was seen in all pancreatic B-cells a few months after birth. The present finding together with the above results suggest that absence of salivary peptide P-C-like immunoreactivity in some foetal pancreatic B-cells may be due to the underdevelopment of salivary peptide P-C-like immunoreactivity in each insulin secretory granule. From the examination of cross-reactivity of antisera against salivary peptide P-C to other kinds of salivary peptides and salivary Protein C, and from the results of an indirect immunofluorescence technique using three kinds of antisera including antisera against salivary peptide P-C, salivary peptide P-B and salivary Protein C, it was thought that salivary peptide P-C-like immunoreactivity in human pancreatic B-cells belongs neither to salivary Protein C nor to salivary peptide P-B nor to salivary peptide P-E, but either to salivary peptide P-C itself or to an unknown substance which has common antigenic determinants with salivary peptide P-C, salivary peptide P-B and salivary Protein C. Salivary peptide P-C-like immunoreactivity was not found in the pancreatic B-cells of other mammals. Thus, although a new substance other than insulin is present in the insulin secretory granules of the human pancreatic B-cells, its pathophysiological function remains unclear.

Adult↗
PubMed1985

Presence of salivary protein C and salivary peptide P-C-like immunoreactivity in the laryngo-tracheo-bronchial glands.

An indirect immunofluorescence technique using antisera against salivary peptide P-C and against salivary Protein C was carried out on the laryngeal, tracheal and bronchial glands to examine whether salivary peptide P-C-like immunoreactivity, recently demonstrated in the serous cells of the human salivary glands, was also present in those of laryngeal, tracheal and bronchial glands and to ascertain whether salivary peptide P-C is a fragment of salivary Protein C or not. Salivary peptide P-C-like immunoreactivity was present in the serous cells of the human laryngeal, tracheal and bronchial glands. Observation of serial sections immunostained with two kinds of antisera revealed that cells reacting with antisera against salivary peptide P-C were identical to those reacting with antisera against salivary Protein C pre-incubated with salivary peptide P-C. The finding implied that salivary peptide P-C and salivary Protein C, originally isolated from human saliva, were also present in the serous cells of tissues other than the salivary glands. Furthermore, analysis of the primary structure of salivary peptide P-C and salivary Protein C together with the present morphological finding suggests that salivary peptide P-C is a COOH-terminal fragment of salivary Protein C. Thus, salivary Protein C and salivary peptide P-C may play some role in the function of the serous cells of the salivary and laryngo-tracheo-bronchial glands.

Bronchi↗
PubMed1984

[A study on salivary peptide P-C with special reference to intracellular localization of salivary peptide P-C like immunoreactivity in the human pancreatic B-cells].

In order to clarify the intracellular localization of salivary peptide P-C like immunoreactivity in the human pancreatic B-cells, an immuno-electronmicroscopical study using protein A-gold technique was carried out on the human foetal pancreas. Salivary peptide P-C like immunoreactivity was present in some of insulin secretory granules while insulin like immunoreactivity was found in all insulin secretory granules. The finding suggested that new substance in addition to insulin and its precursor was present in the insulin secretory granules of the human pancreatic B-cells. Furthermore, the finding seemed to explain the previous study that development of salivary peptide'P-C like immunoreactivity in the foetal pancreatic B-cells was immature in compared to that in the human adult pancreatic B-cells. In addition, to examine whether or not, salivary peptide P-C like immunoreactivity in the human pancreatic B-cells is Salivary Protein C, an indirect immunofluorescence technique using three kinds of antisera against salivary peptide P-C, Salivary Protein C and salivary peptide P-B, and using their antigens was undertaken on the adult pancrease. From the results of the study, it was thought that salivary peptide P-C like immunoreactivity in the human pancreas was neither Salivary Protein C itself, nor salivary peptide P-B itself, but was either salivary peptide P-C itself or unknown substance which had the common antigenic determinant with salivary peptide P-C, P-B and Salivary Protein C, since salivary peptide P-C like immunoreactivity in the human pancreas disappeared in the sections in which P-C antisera preincubated with each of salivary peptide P-C, P-B and Salivary Protein C were used as the primary antisera. Thus, although new substance was present in the insulin secretory granules of the human pancreatic B-cells, its pathophysiological role remained to be elucidated.

Cytoplasmic Granules↗
PubMed1984

[A study on salivary proline-rich peptide P-C with special reference to the presence of salivary peptide P-C in the human respiratory tract].

In order to elucidate whether Salivary Protein C and salivary peptide P-C, originally isolated from human saliva were present in tissues other than those of the salivary glands or not, an indirect immunofluorescence technique using both antisera against salivary peptide P-C and Salivary Protein C was carried out on human salivary glands and the human respiratory tract. As salivary peptide P-C-like immunoreactivity was detected in the serous cells of salivary glands by previous immunohistochemical study, the human respiratory tract was closed as model tissue, since tracheal and bronchial glands in the human respiratory tract consist of mucous and serous cells. Furthermore, to check whether salivary peptide P-C is a fragment of Salivary Protein C or not, the same immunohistochemical study was undertaken on the serial sections of salivary glands and the respiratory tract. Salivary peptide P-C and Salivary Protein C-like immunoreactivities were present in the serous cells of human salivary glands and in tracheal and bronchial cells. Furthermore, the same serous cells were immunostained with antisera against salivary peptide P-C, with antisera against Salivary Protein C and with antisera against Salivary Protein C preabsorbed with salivary peptide P-C. In view of the fact that the full sequence of salivary peptide P-C is identical to the COOH terminal 44 amino acid residues of Salivary Protein C, it was suggested that the full sequence of Salivary Protein C was present in the serous cells of human salivary glands and in those of tracheal and bronchial glands and that salivary peptide P-C was a fragment of Salivary Protein C.(ABSTRACT TRUNCATED AT 250 WORDS)

Bronchi↗
PubMed1984

Primary structure of cat osteocalcin.

A bone Gla-containing protein (osteocalcin) of cat has been isolated and the complete primary structure has been determined to be YLAPGLGAOAPYPDPLXPKRXICXLNPDCDELADHIGFQDAYRRFYGTV. The protein consists of 49 amino acid residues (Mr. 5,641) containing three Gla residues and a single disulfide bond. Although the C-terminal 30 residues (20th to 49th) of the sequences of cow, monkey, and human osteocalcins are identical, three amino acid substitutions occur at positions 22, 40, and 48 in the case of cat. These substitutions can be explained by single point mutations.

Amino Acid Sequence↗
PubMed1984

Isolation and amino acid sequence of SAP-1, an acidic protein of human whole saliva, and sequence homology with human gamma-trace.

A low-molecular-weight acidic protein was isolated from human whole saliva by DE32 column chromatography and designated as SAP-1. The amino acid sequence was determined by conventional methods to be (sequence in text). The protein consisted of 113 residues and the calculated molecular weight was 12,552. Computer analysis revealed the presence of 54% sequence homology between SAP-1 and gamma-trace, a basic microprotein present in cerebrospinal fluid and in urine of patients with renal failure.

Amino Acid Sequence↗
PubMed1984

Cystatin S: a cysteine proteinase inhibitor of human saliva.

An acidic protein of human saliva, which we named SAP-1 previously, is now shown to be an inhibitor of several cysteine proteinases. The protein inhibited papain and ficin strongly, and stem bromelain and bovine cathepsin C partially. However, it did not inhibit either porcine cathepsin B or clostripain. The mode of the inhibition of papain was found to be non-competitive. The name cystatin S has been proposed for this salivary protein in view of the similarities in activity and structure to other cysteine proteinase inhibitors such as chicken egg-white cystatin and human cystatins A, B, and C. The cystatin S antigen was detected immunohistochemically in the serous cells of human parotid and submaxillary glands.

Cystatin A↗
PubMed1984

Conformational study of the basic proline-rich polypeptides from human parotid saliva.

The conformational study of two basic proline-rich polypeptides from human parotid saliva, P--D and P--E of known primary structures, was performed by CD and 1H--n.m.r. spectra measurements. These polypeptides contain consecutive sequences of five prolyl residues in their amino acid sequences. The troughs in CD spectra of P--D and P--E were found at 202 and 201 nm, respectively. These wavelengths were different from the value of 206 nm of poly-L-proline form II conformation. In spite of this, the existence of poly-L-proline form II conformation was suggested in the structure of P--D, because the trough for a fragmental peptide of P--D containing five consecutive prolyl residues was found at 204 nm. No remarkable change was detected in CD and 1H--n.m.r. spectra of P--D and P--E in the range of pH 3.0-11.0. The result suggests that no folding of polypeptide which might be affected by ionic interaction exists in its structure.

Amino Acid Sequence↗