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Biomedical subjects

H Park

Publications and source records attributed to H Park.

At least 325 records · Page 18Linked to original sources
PubMed1987

Mechanisms of mucoadhesion of poly(acrylic acid) hydrogels.

It has been proposed that mucoadhesives which adhere to the gastric mucus layer may be used to prolong gastric retention time of oral dosage forms. Preliminary studies, using acrylic hydrogels, have established that the density of carboxyl groups on the polymer chain is important for mucoadhesion. To understand the role(s) of the carboxyl groups in mucoadhesion, acrylic acid-acrylamide random copolymers [P(AA-co-AM)] were synthesized, and the adhesion strength of the cross-linked polymers to the gastric mucus layer was examined as a function of the pH, initial concentration of the cross-linking agent, degree of swelling, and carboxyl-group density. From the study on mucoadhesion of various P(AA-co-AM), it was found that at least 80% of the vinyl groups of the polymer must possess carboxyl groups in the protonated form. The dependence of mucoadhesion on pH and carboxyl-group density suggests that mucoadhesion occurs through hydrogen bonding. In addition, the density of the cross-linking agent significantly affects mucoadhesion. As the density of the cross-linking agent is lowered, the mucoadhesive strength increases, although the density of carboxyl groups in the test surface area is reduced. It is concluded that for mucoadhesion to occur, polymers must have functional groups that are able to form hydrogen bonds above the critical concentration (80% for vinyl polymers), and the polymer chains should be flexible enough to form as many hydrogen bonds as possible.

Acrylic Resins↗
PubMed1986

Bacterial peptidoglycan induces in vitro rheumatoid factor production by lymphocytes of healthy subjects.

The present studies were carried out to further characterize the polyclonal B cell activating properties of bacterial peptidoglycan (PG) and to determine if this ubiquitous agent induces in vitro IgM rheumatoid factor (RF) production by lymphocytes from healthy volunteers. Peripheral blood mononuclear cells (PBMC) were cultured in the presence of peptidoglycan, pokeweed mitogen (PWM), a standard polyclonal B cell activator, or additional culture medium. Supernatants were harvested on days 7-8 for determination of total IgM, total IgG, and IgM RF by an enzyme-linked immunosorbent assay (ELISA). PG and PWM induced comparable amounts of total IgM production but PG was a less potent stimulant of total IgG production. PG induced in vitro IgM-RF production in 9/33 experiments, a frequency of response of less than that observed in corresponding PWM stimulated cultures (22/33 experiments). PG-induced IgM-RF production depended upon active protein synthesis and did not correlate with the magnitude of PG-induced total IgM production. The latter finding suggests that PG-induced IgM-RF may not merely reflect polyclonal B cell activation. These results add to a growing list of PG's functional properties and provide further impetus for considering this ubiquitous agent as a potential stimulant for in vivo RF production.

Adult↗
PubMed1985

Bioadhesive polymers as platforms for oral controlled drug delivery II: synthesis and evaluation of some swelling, water-insoluble bioadhesive polymers.

A series of cross-linked, swellable polymers was sythesized from monomers such as acrylic acid, methacrylic acid, and others with various cross-linking agents to produce a range of polymers differing in charge densities and hydrophobicity. The densities, rate, and extent of hydration of the polymers were determined. An increase in the number of hydrophobic groups in the polymer structure reduced hydration whereas the density of the polymer was unaffected. A sensitive in vitro method for measuring adhesion of polymer to tissue from the rabbit stomach was developed. Polymers of acrylic acid loosely cross-linked (0.3%, w/w) with three different agents, divinyl glycol, 2,5-dimethyl-1,5-hexadiene, and divinylbenzene, showed the same degree of bioadhesion while poly(methacrylic acid-divinylbenzene) showed reduced bioadhesion. The small percent of cross-linking agent, irrespective of physicochemical properties, did not contribute substantially to bioadhesion, whereas the starting monomer had a large effect. The effect of pH on the bioadhesion of poly(acrylic acid-divinyl glycol) was studied at constant temperature, ionic strength, and osmolality. The polymer showed maximum adhesion at pH 5 and 6 and a minimum at pH 7. Gastrointestinal transit studies of cross-linked polymers in rats were studied. Poly(acrylic acid-divinyl glycol) and poly(methacrylic acid-divinylbenzene) were shown to have substantially longer GI transit times than the control, Amberlite 200 resin beads. The delay in transit time was due to bioadhesion of the polymer to the mucin-epithelial cell surface which was clearly observable on animal autopsy. The acrylic acid polymer showed a longer GI transit time than the methacrylic acid polymer, and this in vivo GI transit result is consistent with in vitro bioadhesion test results.

Acrylic Resins↗
PubMed1984

Detection of soluble peptidoglycan in urine after penicillin administration.

A unique enzyme-linked immunosorbent assay was developed to detect soluble peptidoglycans in biological fluids. It makes use of the similar affinities of vancomycin and purified rabbit antibodies to peptidoglycan precursor sequences found in soluble peptidoglycans. This assay has been used to detect as little as 500 pg of soluble peptidoglycan per ml of serum and 5 pg/ml of urine. Studies of normal individuals and Staphylococcus aureus-infected patients revealed only a few sera with detectable levels of soluble peptidoglycans. Studies of normal volunteers who were given a single oral dose of 250 mg of penicillin VK showed that about half had detectable levels of soluble peptidoglycans in their urine up to 6 h after ingestion. This suggests that soluble peptidoglycans can be released by indigenous bacteria in detectable amounts. In one volunteer, a detectable level of soluble peptidoglycan in the urine at 6 h decreased to an undetectable level at 12 h. Such an ephemeral appearance of soluble peptidoglycan in the urine could account for the small number of human sera that had detectable levels of soluble peptidoglycan.

Adolescent↗
PubMed1984

Antibodies to peptidoglycan in patients with spondylarthritis: a clue to disease aetiology?

Although the aetiology of the spondylarthritic diseases, ankylosing spondylitis and Reiter's syndrome, is obscure, a clue to the pathogenesis might be an animal model, adjuvant arthritis. Rats with this disease develop a spectrum of pathology with marked similarity to the spondylarthritides. Since peptidoglycan, a major cell wall component of most bacteria is causally implicated in adjuvant arthritis, we sought evidence that peptidoglycan exposure accompanies both Reiter's syndrome and ankylosing spondylitis. Antibodies to the D-Ala-D-Ala moiety of peptidoglycan were measured by a sensitive and specific ELISA. Antibodies were elevated significantly in patients with ankylosing spondylitis or Reiter's syndrome, but not in patients with rheumatoid arthritis or degenerative joint disease in comparison with normal controls. The findings should be considered preliminary, since only a minority of patients had increased antibody titres. However, the findings are compatible with the hypothesis that peptidoglycan is causally related to spondylarthritis. Antibodies to other moieties in the peptidoglycan molecule might be a more sensitive test for significant exposure.

Antibodies↗
PubMed1980

Chromosomal mapping of human creatine kinase (brain type) using human-rodent somatic cell hybrids.

Concordant segregation of human brain-type creatine kinase, CK(BB), expression with nucleoside phosphorylase (NP) expression and the presence of chromosome 14 was observed in 53 independently derived cell hybrids between CK(BB)-positive human cells and CK(BB)-negative rodent cells. Further analysis of 26 subclones of two CK(BB)-positive human-mouse cell hybrids confirmed the positive correlation of CK(BB) expression with NP expression. The results suggest that the gene coding for human CK(BB) can be assigned to chromosome 14.

Animals↗