Evidence on the involvement in inflammation of an enzyme resembling aminopeptidase B

Mäkinen, Kauko K.; Oksala, E

doi:10.1016/0009-8981(73)90226-x

Cited by 21 publications

(3 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Even the gingival crevicular fluid may contain sufficiently high Cl -levels to be utilized by peptidases present in periodontopathic treponemes [9]. A mammalian enzyme, aminopeptidase B (EC 3.4.11.6), suggested to play a role in the extracellular inflammatory processes, is specifically activated by physiological [Cl -] [30,31]. The above Cl -effects can be used as an additional identification procedure of spirochetal peptidases.…”

Section: Selective Effect Of CL -mentioning

confidence: 98%

The peptidolytic capacity of the spirochete system

Mäkinen

Mäkinen²

1996

Med Microbol Immunol

View full text Add to dashboard Cite

Relatively scant chemical information has been available on the proteinases and peptidases of spirochetes in spite of the association of spirochetes with several serious infections known to plague humans and other animal species. This situation has partly resulted from difficulties in growing some spirochetes under laboratory conditions. The cells of Treponema denticola, a spirochete suggested to be associated with periodontal infections, have turned out to be a good source of new chemical information on those enzymes. Latest studies suggest that the outer cell envelope or the periplasmic space of T. denticola contains several novel proteinases and peptidases (hence called "ectoenzymes") which may contribute to the chronicity of periodontal infections. Some of the oligopeptidases discovered are specific for proline-containing host tissue peptides such as substance P, bradykinin, neurotensin, etc., and possibly small collagen fragments. The only spirochetal peptidases purified to give a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis have been obtained from T. denticola. One particular peptidase, suggested to be similar to the oligopeptidase B (EC 3.4.21.83) of Escherichia coli seems to be present in the cell envelope or in the periplasmic space at quite large concentrations. The presence of this and several other peptidases in the outer cell structures of the treponemes suggests that such enzymes are important for the nutrition of these highly motile and invasive organisms. The biological role of these enzymes can thus be envisaged in the peptidolytic processing of host tissue proteins and peptides to gradually smaller molecules to fulfill the nutritional requirements of these organisms. Although the genetic similarity between T. denticola and some other treponemes and spirochetes can be hotly debated, it is nevertheless now possible to use T. denticula enzymes as suitable objects for comparison when the chemistry of other spirochetes is studied.

show abstract

Section: Selective Effect Of CL -mentioning

confidence: 98%

The peptidolytic capacity of the spirochete system

Mäkinen

Mäkinen²

1996

Med Microbol Immunol

View full text Add to dashboard Cite

show abstract

“…This metabolite is a potent inhibitor of leucine aminopeptidase and aminopeptidase B of mammalian cells [18,29,30] and immune cells both in vitro [17,19,22,36] and in vivo [15]. Aminopeptidase activity has been associated with macrophage activation and differentiation [21,37], the inflammatory process [20,23,28] and was shown in a cell-free system to correlate *This research was sponsored by the National Cancer Institute, DHHS, under contract no. N01-23910 with Program Resources Inc.…”

Section: Introductionmentioning

confidence: 99%

Chemoimmunotherapy with cyclophosphamide and bestatin in experimental metastasis in mice

Abe

Schneider²,

Black

et al. 1989

Cancer Immunol Immunother

View full text Add to dashboard Cite

Bestatin has significant therapeutic activity (even following oral administration) for the treatment of metastatic disease, an activity which is limited by tumor burden. Therefore, the therapeutic potential of bestatin was examined in combination with chemotherapy to determine if there is additive activity for heavy tumor burdens. Bestatin significantly increased therapeutic activity and decreased the myelotoxicity of cyclophosphamide following a single injection of cyclophosphamide or split daily doses. In immune function studies, in tumor-bearing animals, bestatin increased the number of colony-forming units (granulocyte-macrophage) (CFU) and alveolar macrophage tumoricidal activity. However, when bestatin was combined with cyclophosphamide, which depressed bone marrow and macrophage activity, it did not show apparent augmentation of macrophage and NK cell activity, but did significantly increase bone marrow CFU activity. Thus, in combined chemoimmunotherapy, bestatin appears to enhance therapeutic activity by accelerating the recovery of hematopoiesis. We suggest, therefore, that a combination chemotherapy protocol, with oral bestatin, may facilitate myelorestoration following aggressive chemotherapy. The majority of biological response modifiers require parental administration; thus, the identification of an orally active, synthetic immunoaugmenting agent with a defined receptor is of particular interest.

show abstract

“…In order to reveal the involvement of specific Cl"-dependent arginine aminopeptidases (EC 3.4,11.6) (5, 6), the hydrolysis of Arg-2-NA was tested in the presence of 0.2 M NaCl and without added salt. Our previous studies on the NaCl effects of aminopeptidases have shown that 0.2 M NaCl can be used to differentiate between Cl~-dcpendent and Cl"inhibitcd enzymes (7)(8)(9)(10)(11).…”

Section: Methodsmentioning

confidence: 99%

Effect of xylitol‐, sucrose‐, and water‐rinses on the composition of human palatine gland secretions

Mäkinen

Virtanen

Söderling

et al. 1985

European J Oral Sciences

Self Cite

View full text Add to dashboard Cite

– The chemical composition of stimulated human palatine secretions (HPS) was studied after rinsing with aqueous solutions of sucrose or xylitol, or with water only. Stimulation with water was associated with increased concentration levels of protein. The levels of sialic acids (per mg protein) and the specific arylamidase activities were simultaneously increased, within the physiologic range. In contrast to a previous report, these results indicate that HPS does contain arylaminopeptidases the activity of which is strongly increased by Cl−, The Cl− ‐dependent activity was revealed when using N‐L‐arginyl‐2‐naphthylamide as substrate. The filter paper method used is recommended for collecting HPS for chemical analyses. In spite of the use of a relatively effective and versatile stimulation procedure, only one third of the subjects produced detectable HPS, Very poor secretion of HPS should perhaps be considered in subjects wearing total dentures.

show abstract

Evidence on the involvement in inflammation of an enzyme resembling aminopeptidase B

Cited by 21 publications

References 17 publications

The peptidolytic capacity of the spirochete system

The peptidolytic capacity of the spirochete system

Chemoimmunotherapy with cyclophosphamide and bestatin in experimental metastasis in mice

Effect of xylitol‐, sucrose‐, and water‐rinses on the composition of human palatine gland secretions

Contact Info

Product

Resources

About