Novel antiproliferative factor and methods of use

a technology of antiproliferative factor and anti-proliferative agent, which is applied in the field of biochemistry, cell biology, chemistry, can solve the problems of loss of epithelial barrier integrity, unfavorable conventional methods of structural analysis, such as nmr spectroscopy, and achieve the effect of improving sensitivity to a cancer therapy, facilitating or facilitating the overcoming of resistan

Inactive Publication Date: 2005-05-05
HEALTH & HUMAN SERVICES THE GOVERNMENT OF THE US SEC THE DEPT OF +1
View PDF7 Cites 47 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0036] The present invention is directed to methods of treating cancer comprising administering an effective amount of APF or derivatives thereof to a patient in need of such treatment. Any kind of cancer may be treated, such as bladder, lung, breast, prostate, brain, stomach, colon, spleen, liver, pancreatic, melanoma, head and neck, thyroid, and so forth. In specific embodiments, though, the invention is use

Problems solved by technology

These findings suggest that interstitial cystitis may be caused by an inhibition of normal bladder epithelial cell proliferation, resulting in a loss of epithelial barrier integrity with subsequent exposure of sensory nerve cells in the bl

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Novel antiproliferative factor and methods of use
  • Novel antiproliferative factor and methods of use
  • Novel antiproliferative factor and methods of use

Examples

Experimental program
Comparison scheme
Effect test

example 1

Examplary Methods and Reagents

Cell Cultures

[0199] Cystoscopy was performed under general anesthesia, and 4 mm2 pieces of transitional epithelium with submucosa bladder tissue were obtained using rigid cold cup biopsy forceps from six patients who had previously undergone cystoscopy and fulfilled the NIDDK / NIH diagnostic criteria for interstitial cystitis, and six age- race- and gender-matched controls who were asymptomatic for urinary tract disease, as previously described (Keay et al., 2001; Keay et al., 2000; Keay et al., 2003a; Keay et al., 2003b; Keay et al., 1996). All patients were at least 18 years old and enrolled in accordance with guidelines of the Institutional Review Board of the University of Maryland School of Medicine.

[0200] Explanted epithelial cells were propagated from these biopsy specimens in DMEM-F12 (Media Tech, Herndon, Va.) with 10% heat inactivated fetal bovine serum (FBS), 1% antibiotic / antimycotic solution, 1% L-glutamine, 1.0 U / ml insulin (all from Si...

example 2

Identification of Amino Acids by Mass Spectometric Analysis

[0221] In specific aspects of the invention, an APF molecule is identified and / or characterized by any suitable means in the art, such as through the characterization of the peptide, sugar, or glycopeptide moiety of APF. In one specific embodiment, mass spectrometry is utilized. In other embodiments, techniques such as nuclear magnetic resonance or proteomic techniques (including isotope-coded affinity assays), and sensitive chromatographic methods may be utilized, for example.

[0222] Microcapillary reversed-phase liquid chromatography was used to obtain extremely pure preparations of APF peptide for mass spectrometry. Analysis of three preparations of HPLC-purified APF using the microcapillary technique indicated the presence of three peptide peaks in approximately equal proportions in each preparation, only one of which had antiproliferative activity against primary bladder epithelial cells in vitro. Ion trap mass spectro...

example 3

Identification of Sugar Moieties by Lectin Binding Analysis

[0235] In specific aspects of the invention, an APF molecule is identified and / or characterized by any suitable means in the art. In one specific embodiment, lectin binding analysis is utilized to identify sugar moieties. Other methods for sugar identification including, but not limited to, chemical degradation, NMR spectroscopy, mass spectrometry, and antibody binding can also be used to identify sugar moieties.

[0236] To determine the identity and linkage of the hexose and hexosamine moieties, HPLC-purified APF was incubated in its native state with various agarose-conjugated lectins and the eluates tested for antiproliferative activity (Table 2).

TABLE 2Lectin Binding AnalysisAPF BindingNeuraminidase-LectinReported SpecificityNativetreatedWheat germ agglutininsialic acid; terminal+NDGlcNAcTritrichomonassialic acid+NDPeanut agglutininGalβ1-3GalNAc;−+GalactoseConcanavalin AMannose, Glucose−−Lentil lectinMannose, Glucose;−...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

PropertyMeasurementUnit
Lengthaaaaaaaaaa
Compositionaaaaaaaaaa
Polarityaaaaaaaaaa
Login to view more

Abstract

A novel antiproliferative factor comprising a glycopeptide is disclosed. In specific embodiments, the novel antiproliferative factor is associated with the bladder. Compositions, diagnostic kits and reagents, and methods of using the compounds for identifying and/or treating interstitial cystitis and cancer are disclosed.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application claims priority to U.S. Provisional Patent Application Ser. No. 60 / 484,010, filed Jul. 1, 2003; U.S. Provisional Patent Application Ser. No. 60 / 515,850, filed Oct. 29, 2003; and U.S. Provisional Patent Application Ser. No. 60 / 569,363, filed May 7, 2004, all of which are incorporated by reference herein in their entirety.STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH OR DEVELOPMENT [0002] The present invention was generated at least in part with funds from National Institutes of Health NIH, NIDDK DK52596; the Veterans Administration (VA Merit Review Funding); and intramural National Cancer Institute funds. The United States Government may have certain rights in the invention.FIELD OF THE INVENTION [0003] The present invention is directed to fields of medicine, biochemistry, cell biology, and chemistry. More specifically, the present invention addresses a novel compound and derivatives thereof having growth inhibitory a...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
IPC IPC(8): A61K38/18
CPCC07K9/005A61K38/00
Inventor KEAY, SUSANMICHEJDA, CHRISTOPHERSZEKELY, ZOLTAN
Owner HEALTH & HUMAN SERVICES THE GOVERNMENT OF THE US SEC THE DEPT OF
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap