# US 2015/0147762 A1 · Method for detecting cancer, and antibody capable of recognizing pancreatic ribonuclease 1 > Agents: this data is available as JSON from the patentgrep API and MCP server — see https://patentgrep.com/llms.txt - Number: US 2015/0147762 A1 - Document ID: US20150147762A1 - Status: Published application - Kind: A1 - Application number: 14/406,445 - Filed: 2013-06-06 - Published: 2015-05-28 - Earliest claimed: 2012-06-11 - Assignees: Tosoh Corporation - Applicants: Tosoh Corporation - Inventors: Daisuke Nakatani - Web page: https://patentgrep.com/patent/US20150147762A1 ## CPC - G01N 33/57525: of the liver or pancreas - A61P 1/18: for pancreatic disorders, e.g. pancreatic enzymes - A61P 35/00: Antineoplastic agents - C07K 16/303: {Liver or Pancreas} - C07K 16/40: against enzymes - G01N 33/57585: {involving compounds identifiable in body fluids} - C07K 2317/30: characterized by aspects of specificity or valency - C07K 2317/34: Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues - G01N 2333/922: Ribonucleases (RNAses); Deoxyribonucleases (DNAses) - G01N 2440/38: addition of carbohydrates, e.g. glycosylation, glycation - G01N: INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES (measuring or testing apparatus or processes other than immunoassay, involving enzymes or microorganisms C12M, C12Q) - A61P: SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS - C07K: PEPTIDES (peptides in foodstuffs A23; obtaining protein compositions for foodstuffs, working-up proteins for foodstuffs A23J; preparations for medicinal purposes A61K; peptides containing beta-lactam rings C07D; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, C07D; ergot alkaloids of the cyclic peptide type C07D519/02; macromolecular compounds having statistically distributed amino acid units in their molecules, i.e. when the preparation does not provide for a specific; but for a random sequence of the amino acid units, homopolyamides and block copolyamides derived from amino acids C08G69/00; macromolecular products derived from proteins C08H1/00; preparation of glue or gelatine C09H; single cell proteins, enzymes C12N; genetic engineering processes for obtaining peptides C12N15/00; compositions for measuring or testing processes involving enzymes C12Q; investigation or analysis of biological material G01N33/00) ## Abstract Pancreatic cancer can be detected using a monoclonal antibody which binds to pancreatic RNase 1 when a site in pancreatic RNase 1 capable of being modified with an N-glycan chain is not linked to a glycan chain, but which does not bind to pancreatic RNase 1 when an N-glycan chain is linked to the site. Also provided is a monoclonal antibody which can bind to pancreatic RNase 1 simultaneously with the binding of the aforementioned antibody to pancreatic RNase 1, and determining the ratio of A to B using the antibodies, wherein A represents the amount of the site located in the pancreatic RNase 1 capable of being modified with an N-glycan chain, wherein an N-glycan chain is linked or not linked to the site; and B represents the amount of the site located in the pancreatic RNase 1 capable of being modified with an N-glycan chain. ## Claims ### Claim 1 A method for detecting cancer, characterized by measuring the amount of a putative N-glycosylation site of a glycoprotein linked with an N-glycan chain or not linked with an N-glycan chain. ### Claim 2 (depends on 1) The method according to claim 1, wherein the cancer is pancreatic cancer. ### Claim 3 (depends on 1) The method according to claim 1, wherein the glycoprotein is pancreatic ribonuclease 1. ### Claim 4 (depends on 2) The method according to claim 2, wherein the amount of the site linked with the N-glycan chain is increased in pancreatic cancer patients in comparison with healthy individuals. ### Claim 5 A method for detecting cancer, comprising: determining the ratio A/B for A and B indicated below: A: amount of putative N-glycosylation site of a glycoprotein linked with an N-glycan chain or not linked with an N-glycan chain; and, B: amount of putative N-glycosylation site of the glycoprotein. ### Claim 6 (depends on 5) The method according to claim 5, wherein the cancer is pancreatic cancer. ### Claim 7 (depends on 5) The method according to claim 5, wherein the glycoprotein is pancreatic ribonuclease 1. ### Claim 8 (depends on 6) The method according to claim 6, wherein A represents the amount of the site not linked with an N-glycan chain, and the value of A/B is smaller in pancreatic cancer patients in comparison with healthy individuals. ### Claim 9 (depends on 6) The method according to claim 6, wherein A represents the amount of the site linked with an N-glycan chain, and the value of A/B is larger in pancreatic cancer patients in comparison with healthy individuals. ### Claim 10 (depends on 7) The method according to claim 7, wherein the amount of pancreatic RNase 1 is determined and that value is converted and used as the value of B. ### Claim 11 (depends on 1) The method according to claim 1, wherein the putative N-glycosylation site is one or more asparagine residues selected from asparagine at positions 34, 76 and 88 of the sequence indicated in SEQ ID NO: 4. ### Claim 12 (depends on 11) The method according to claim 11, wherein the putative N-glycosylation site is an asparagine residue at position 88 of the sequence indicated in SEQ ID NO: 4. ### Claim 13 (depends on 11) The method according to claim 11, wherein the putative N-glycosylation site is an asparagine residue at position 76 of the sequence indicated in SEQ ID NO: 4. ### Claim 14 (depends on 11) The method according to claim 11, wherein the putative N-glycosylation site is an asparagine residue at position 34 of the sequence indicated in SEQ ID NO: 4. ### Claim 15 A monoclonal antibody, or fragment thereof, recognizing a putative N-glycosylation site of pancreatic RNase 1 as a portion of the antigen recognition site thereof. ### Claim 16 (depends on 15) The monoclonal antibody, or fragment thereof, according to claim 15, wherein binding to the putative N-glycosylation site of pancreatic RNase 1 occurs in the case the site is not linked with an N-glycan chain, and is inhibited in the case the site is linked with an N-glycan chain. ### Claim 17 (depends on 15) The monoclonal antibody, of fragment thereof, according to claim 15, wherein the antigen recognition site is a region that contains an asparagine residue at position 88 of the sequence indicated in SEQ ID NO: 4. ### Claim 18 (depends on 15) A monoclonal antibody or fragment thereof capable of binding to pancreatic RNase 1 simultaneous to the monoclonal antibody, or fragment thereof, according to claim 15. ### Claim 19 (depends on 1) The method according to claim 1, comprising contacting a monoclonal antibody or fragment thereof, recognizing a putative N-glycosylation site of pancreatic RNase 1 as a portion of the antigen recognition site thereof (a) with a sample, and measuring the amount of pancreatic RNase 1 that has formed a complex with the monoclonal antibody or a fragment thereof represented with (a). ### Claim 20 (depends on 19) The method according to claim 19, comprising further contacting a monoclonal antibody or fragment thereof capable of binding to pancreatic RNase 1 simultaneous to the monoclonal antibody, or fragment thereof (b) with the sample and measuring the amount of pancreatic RNase 1 that has formed a complex with the two monoclonal antibodies or fragments thereof represented with (a) and (b). ### Claim 21 (depends on 20) The method according to claim 20, comprising a first contact step for contacting the sample with (a) or (b), and a second contact step for contacting the other (a) or (b) with that obtained in the first contact step. ### Claim 22 (depends on 15) A pharmaceutical containing the monoclonal antibody, or fragment thereof, according to claim 15. ### Claim 23 (depends on 1) The method according to claim 1, wherein the amount of the putative N-glycosylation site of the glycoprotein linked with N-glycan chain or not linked with the N-glycan chain is determined by mass spectrometry. ### Claim 24 (depends on 23) The method according to claim 23, wherein the mass of a peptide fragment and/or glycopeptide fragment of a glycoprotein is measured by mass spectrometry.