{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:45:36Z","timestamp":1791852336349,"version":"4.3.4"},"reference-count":38,"publisher":"MDPI AG","issue":"19","license":[{"start":{"date-parts":[[2023,9,22]],"date-time":"2023-09-22T00:00:00Z","timestamp":1695340800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Lysozyme amyloidosis is caused by an amino acid substitution in the sequence of this protein. In our study, we described a clinical case of lysozyme amyloidosis in a Russian family. In our work, we described in detail the histological changes in tissues that appeared as a result of massive deposition of amyloid aggregates that affected almost all organ systems, with the exception of the central nervous system. We determined the type of amyloidosis and mutations using mass spectrometry. Using mass spectrometry, the protein composition of tissue samples of patient 1 (autopsy material) and patient 2 (biopsy material) with histologically confirmed amyloid deposits were analyzed. Amino acid substitutions p.F21L\/T88N in the lysozyme sequence were identified in both sets of samples and confirmed by sequencing of the lysozyme gene of members of this family. We have shown the inheritance of these mutations in the lysozyme gene in members of the described family. For the first time, we discovered a mutation in the first exon p.F21L of the lysozyme gene, which, together with p.T88N amino acid substitution, led to amyloidosis in members of the studied family.<\/jats:p>","DOI":"10.3390\/ijms241914453","type":"journal-article","created":{"date-parts":[[2023,9,24]],"date-time":"2023-09-24T10:36:26Z","timestamp":1695551786000},"page":"14453","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["First Report of Lysozyme Amyloidosis with p.F21L\/T88N Amino Acid Substitutions in a Russian Family"],"prefix":"10.3390","volume":"24","author":[{"given":"Mariya Yu.","family":"Suvorina","sequence":"first","affiliation":[{"name":"Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena A.","family":"Stepanova","sequence":"additional","affiliation":[{"name":"Federal State Budgetary Educational Institution of Further Professional Education \u201cRussian Medical Academy of Continuous Professional Education\u201d of the Ministry of Healthcare of the Russian Federation, 125993 Moscow, Russia"},{"name":"State Budgetary Healthcare Institution \u201cCity Clinical Hospital named after V.M. Buyanov of Moscow Healthcare Department\u201d, 115516 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vilen V.","family":"Rameev","sequence":"additional","affiliation":[{"name":"Tareev\u2019s Clinic of Internal, Occupational Diseases and Rheumatology, Sechenov\u2019s First Moscow State Medical University, 119021 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lidiya V.","family":"Kozlovskaya","sequence":"additional","affiliation":[{"name":"Tareev\u2019s Clinic of Internal, Occupational Diseases and Rheumatology, Sechenov\u2019s First Moscow State Medical University, 119021 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anatoly S.","family":"Glukhov","sequence":"additional","affiliation":[{"name":"Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anastasiya A.","family":"Kuznitsyna","sequence":"additional","affiliation":[{"name":"Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexey K.","family":"Surin","sequence":"additional","affiliation":[{"name":"Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia"},{"name":"Branch of the Shemyakin\u2013Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia"},{"name":"State Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3962-1520","authenticated-orcid":false,"given":"Oxana V.","family":"Galzitskaya","sequence":"additional","affiliation":[{"name":"Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia"},{"name":"Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,9,22]]},"reference":[{"key":"ref_1","first-page":"253","article-title":"Demonstration Einer Eigenartigen Familiaren Paraamyloidose [Demonstration of a Peculiar Hereditary Amyloidosis]","volume":"56","author":"Ostertag","year":"1932","journal-title":"Zentralbl. Aug. Pathol."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Li, Z., Xu, H., Liu, D., Li, D., Liu, G., and Wang, S.-X. (2019). Hereditary Renal Amyloidosis with a Variant Lysozyme p.Trp82Arg in a Chinese Family: Case Report and Literature Review. BMC Nephrol., 20.","DOI":"10.1186\/s12882-019-1496-6"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1046\/j.1523-1755.2002.00205.x","article-title":"Hereditary Renal Amyloidosis Caused by a New Variant Lysozyme W64R in a French Family","volume":"61","author":"Valleix","year":"2002","journal-title":"Kidney Int."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/362553a0","article-title":"Human Lysozyme Gene Mutations Cause Hereditary Systemic Amyloidosis","volume":"362","author":"Pepys","year":"1993","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1681\/ASN.2016090951","article-title":"Hereditary Lysozyme Amyloidosis Variant p.Leu102Ser Associates with Unique Phenotype","volume":"28","author":"Nasr","year":"2017","journal-title":"JASN"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1002\/1098-1004(200008)16:2<180::AID-HUMU20>3.0.CO;2-#","article-title":"A Novel Variant of Human Lysozyme (T70N) Is Common in the Normal Population","volume":"16","author":"Booth","year":"2000","journal-title":"Hum. Mutat."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1002\/humu.9393","article-title":"ALys Amyloidosis Caused by Compound Heterozygosity in Exon 2 (Thr70Asn) and Exon 4 (Trp112Arg) of the Lysozyme Gene","volume":"27","author":"Becker","year":"2006","journal-title":"Hum. Mutat."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1053\/gast.2002.36022","article-title":"A Family with Gastrointestinal Amyloidosis Associated with Variant Lysozyme","volume":"123","author":"Granel","year":"2002","journal-title":"Gastroenterology"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1080\/13506129.2022.2072198","article-title":"Lysozyme Amyloidosis-a Report on a Large German Cohort and the Characterisation of a Novel Amyloidogenic Lysozyme Gene Variant","volume":"29","author":"Anker","year":"2022","journal-title":"Amyloid"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"182","DOI":"10.3109\/13506129.2012.723074","article-title":"A New Lysozyme Tyr54asn Mutation Causing Amyloidosis in a Family of Swedish Ancestry with Gastrointestinal Symptoms","volume":"19","author":"Girnius","year":"2012","journal-title":"Amyloid"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1652","DOI":"10.1046\/j.1523-1755.2003.00904.x","article-title":"A Novel Lysozyme Mutation Phe57Ile Associated with Hereditary Renal Amyloidosis","volume":"63","author":"Yazaki","year":"2003","journal-title":"Kidney Int."},{"key":"ref_12","first-page":"69","article-title":"Familial Amyloidosis Associated with a Novel Mutation (D67G) in the Lysozyme Gene","volume":"13","author":"Woolliver","year":"2006","journal-title":"Amyloid"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2623","DOI":"10.1007\/s10067-017-3839-7","article-title":"Hereditary Lysozyme Amyloidosis with Sicca Syndrome, Digestive, Arterial, and Tracheobronchial Involvement: Case-Based Review","volume":"36","author":"Benyamine","year":"2017","journal-title":"Clin. Rheumatol."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Jean, E., Ebbo, M., Valleix, S., Benarous, L., Heyries, L., Grados, A., Bernit, E., Grateau, G., Papo, T., and Granel, B. (2014). A New Family with Hereditary Lysozyme Amyloidosis with Gastritis and Inflammatory Bowel Disease as Prevailing Symptoms. BMC Gastroenterol., 14.","DOI":"10.1186\/1471-230X-14-159"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1080\/13506129.2016.1269738","article-title":"Complex p.T88N\/W130R Mutation in the Lysozyme Gene Leading to Hereditary Lysozyme Amyloidosis with Biopsy-Proven Cardiac Involvement","volume":"24","author":"Sperry","year":"2017","journal-title":"Amyloid"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1908","DOI":"10.1002\/lt.20984","article-title":"Emergency Liver Transplantation for Hereditary Lysozyme Amyloidosis","volume":"12","author":"Mells","year":"2006","journal-title":"Liver Transpl."},{"key":"ref_17","first-page":"42","article-title":"Lysozyme Amyloidosis\u2014A Case Report and Review of the Literature","volume":"3","author":"Pleyer","year":"2015","journal-title":"Clin. Nephrol. Case Stud."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1080\/13506120701260224","article-title":"Diagnostic Performance of Amyloid A Protein Quantification in Fat Tissue of Patients with Clinical AA Amyloidosis","volume":"14","author":"Hazenberg","year":"2007","journal-title":"Amyloid"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.3324\/haematol.2013.102764","article-title":"Clinical Diagnosis and Typing of Systemic Amyloidosis in Subcutaneous Fat Aspirates by Mass Spectrometry-Based Proteomics","volume":"99","author":"Vrana","year":"2014","journal-title":"Haematologica"},{"key":"ref_20","first-page":"616","article-title":"Comparison of Experimental and Theoretical Data on Hydrogen-Deuterium Exchange for Ten Globular Proteins","volume":"77","author":"Suvorina","year":"2012","journal-title":"Biochemistry"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"5960","DOI":"10.1016\/j.csbj.2021.10.036","article-title":"Is There an Advantageous Arrangement of Aromatic Residues in Proteins? Statistical Analysis of Aromatic Interactions in Globular Proteins","volume":"19","author":"Lobanov","year":"2021","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Lobanov, M.Y., Slizen, M.V., Dovidchenko, N.V., Panfilov, A.V., Surin, A.A., Likhachev, I.V., and Galzitskaya, O.V. (2023). Comparison of Deep Learning Models with Simple Method to Assess the Problem of Antimicrobial Peptides Prediction. Mol. Inf. Inform., e2200181.","DOI":"10.1002\/minf.202200181"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1002\/prot.10104","article-title":"Increasing the Precision of Comparative Models with YASARA NOVA-a Self-Parameterizing Force Field","volume":"47","author":"Krieger","year":"2002","journal-title":"Proteins"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"3098","DOI":"10.1093\/bioinformatics\/btx345","article-title":"Protein\u2013Sol: A Web Tool for Predicting Protein Solubility from Sequence","volume":"33","author":"Hebditch","year":"2017","journal-title":"Bioinformatics"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Pak, M.A., Dovidchenko, N.V., Sharma, S.M., and Ivankov, D.N. (2023). New Mega Dataset Combined with Deep Neural Network Makes a Progress in Predicting Impact of Mutation on Protein Stability. Bioinformatics, 2.","DOI":"10.1101\/2022.12.31.522396"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Conchillo-Sol\u00e9, O., De Groot, N.S., Avil\u00e9s, F.X., Vendrell, J., Daura, X., and Ventura, S. (2007). AGGRESCAN: A Server for the Prediction and Evaluation of \u201cHot Spots\u201d of Aggregation in Polypeptides. BMC Bioinform., 8.","DOI":"10.1186\/1471-2105-8-65"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1093\/bioinformatics\/btp691","article-title":"FoldAmyloid: A Method of Prediction of Amyloidogenic Regions from Protein Sequence","volume":"26","author":"Garbuzynskiy","year":"2010","journal-title":"Bioinformatics"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/nmeth.1432","article-title":"Exploring the Sequence Determinants of Amyloid Structure Using Position-Specific Scoring Matrices","volume":"7","author":"Debulpaep","year":"2010","journal-title":"Nat. Methods"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"W301","DOI":"10.1093\/nar\/gku399","article-title":"PASTA 2.0: An Improved Server for Protein Aggregation Prediction","volume":"42","author":"Walsh","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/0014-5793(71)80506-9","article-title":"The Major Proteins of Human and Monkey Amyloid Substance: Common Properties Including Unusual N-Terminal Amino Acid Sequences","volume":"19","author":"Benditt","year":"1971","journal-title":"FEBS Lett."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1126\/science.172.3988.1150","article-title":"Amyloid Fibril Proteins: Proof of Homology with Immunoglobulin Light Chains by Sequence Analyses","volume":"172","author":"Glenner","year":"1971","journal-title":"Science"},{"key":"ref_32","unstructured":"Serov, V.V., and Shamov, I.A. (1977). Amyloidosis. Medicine, 288."},{"key":"ref_33","unstructured":"Nazarov, P.G. (2001). Acute phase reactants of inflammation. Nauka, 423."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1007\/BF01254559","article-title":"Imaging Amyloidosis with Radiolabelled SAP","volume":"22","author":"Hawkins","year":"1995","journal-title":"Eur. J. Nucl. Med."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Jarvis, S., and Mostaert, A. (2012). The Functional Fold: Amyloid Structures in Nature, Pan Stanford.","DOI":"10.1201\/b12776"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/s41467-023-35854-0","article-title":"Cryo-EM Structure of HnRNPDL-2 Fibrils, a Functional Amyloid Associated with Limb-Girdle Muscular Dystrophy D3","volume":"14","author":"Visentin","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1080\/13506129.2022.2147636","article-title":"Amyloid Nomenclature 2022: Update, Novel Proteins, and Recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee","volume":"29","author":"Buxbaum","year":"2022","journal-title":"Amyloid"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1016\/S0021-9258(19)75212-0","article-title":"Peptide Mapping by Limited Proteolysis in Sodium Dodecyl Sulfate and Analysis by Gel Electrophoresis","volume":"252","author":"Cleveland","year":"1977","journal-title":"J. Biol. Chem."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/19\/14453\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T20:56:08Z","timestamp":1760129768000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/19\/14453"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,9,22]]},"references-count":38,"journal-issue":{"issue":"19","published-online":{"date-parts":[[2023,10]]}},"alternative-id":["ijms241914453"],"URL":"https:\/\/doi.org\/10.3390\/ijms241914453","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,9,22]]}}}