( 0 (51) International Patent Classification: Published: C12N 9/00 (2006.0 1) Cl 2 1/48 (2006.0 1) — with international search report (Art. 21(3)) C07K14/52 (2006.01) G01N 33/573 (2006.01) — with sequence listing part of description (Rule 5.2(a)) (21) International Application Number: PCT/US2020/02008 1 (22) International Filing Date: 27 February 2020 (27.02.2020) (25) Filing Language: English (26) Publication Language: English (30) Priority Data: 62/81 1,135 27 February 2019 (27.02.2019) US (71) Applicant: THE REGENTS OF THE UNIVERSITY OF MICHIGAN [US/US]; 1600 Huron Parkway, 2nd Floor, Ann Arbor, Michigan 48109-2590 (US). (72) Inventors: OMARY, Bishr; c/o The Regents of the Uni¬ versity of Michigan, 1600 Huron Parkway, 2nd Floor, Ann Arbor, Michigan 48109-2590 (US). PARK, Min-Jung; c/ o The Regents of the University of Michigan, 1600 Huron Parkway, 2nd Floor, Ann Arbor, Michigan 48109-2590 (US). (74) Agent: STAPLE, David W.; Casimir Jones, S.C., 2275 Deming Way, Ste 310, Middleton, Wisconsin 53562 (US). (81) Designated States (unless otherwise indicated, for every kind of national protection available) : AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, HR, HU, ID, IL, IN, IR, IS, JO, JP, KE, KG, KH, KN, KP, KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, SC, SD, SE, SG, SK, SL, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, WS, ZA, ZM, ZW. (84) Designated States (unless otherwise indicated, for every kind of regional protection available) : ARIPO (BW, GH, GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, EE, ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, SM, TR), OAPI (BF, BJ, CF, CG, Cl, CM, GA, GN, GQ, GW, KM, ML, MR, NE, SN, TD, TG). (54) Title: CARBAMOYL PHOSPHATE SYNTHETASE-1 FOR THE TREATMENT AND PREVENTION OF LIVER INJURY (57) Abstract: Provided herein are compositions methods for the treatment and/or prevention of liver injury. In particular, carbamoyl phosphate synthetase-1 (CPS-I) peptides and polypeptides (e.g., enzymatically active or inactive CPS-I peptides and polypeptides), and methods of use thereof for the treatment and/or prevention of liver injury are provided. CARBAMOYL PHOSPHATE SYNTHETASE-1 FOR THE TREATMENT AND PREVENTION OF LIVER INJURY STATEMENT REGARDING FEDERAL FUNDING This invention was made with government support under DK047918 awarded by the National Institutes of Health. The government has certain rights in the invention. FIELD Provided herein are compositions methods for the treatment and/or prevention of liver injury. In particular, carbamoyl phosphate synthatase-1 (CPS1) peptides and polypeptides (e.g., enzymatically active or inactive CPS1 peptides and polypeptides), and methods of use thereof for the treatment and/or prevention of liver injury are provided. BACKGROUND Acute liver failure (ALF) is a life-threatening illness defined by rapid deterioration in liver function frequently resulting in diverse clinical features including hepatic encephalopathy and bleeding diathesis. Approximately 2,000 people develop ALF annually in the United States, and more than half of the cases are caused by drug-induced liver injury, particularly overdoses with acetaminophen (APAP), with other etiologies including viral infection, alcoholic hepatitis, other drug reactions, and hepatic ischemia (Bernal W and Wendon J (2013) N Engl JMed 369:2525-2534.; Lee WM (2013) Clin Liver Dis 17, 575-86.; herein incorporated by reference in their entireties). Many different proteins, called alarmins or damage-associated molecular patterns (DAMPs), are released during liver and other tissue injury and are involved in disease progression. For example, high-mobility group box-1 (HMGB1) is the prototypic DAMP protein released during diverse context of damage (Antoine DJ et al. (2012) J Hepatol 56: 1070-1079.; Ilmakunnas M . et al. (2008) Liver Transpl 14:1517-1525.; Kostova et al. (2010). Mol Cell Biochem 337:251-258.; Yan W et al. (2012) Hepatology 55:1863-1875.; herein incorporated by reference in their entireties). HMGB1 functions as a DNA chaperone in the nucleus; however, upon release, it triggers the secretion of pro-inflammatory cytokines through binding to toll-like receptor-4 (TLR4) or the receptor for advanced glycation end products (RAGE) (Bianchi ME et al. (2017) Immunol Rev 280:74-82.; herein incorporated by reference in its entirety). Inner mitochondrial membrane cytochrome c is another protein found in the extracellular space under pathological condition with a potential role as a DAMP (Eleftheriadis et al. (2016) Front Immunol 7:279.; Miller TJ et al. (2008) J Appl Toxicol28:815-828.; herein incorporated by reference in their entireties). Moreover, DNA, RNA and mitochondrial DNA are also considered as DAMPs (Chen GY, and Nunez G (2010) Nat Rev Immunol 10:826-837.; Szabo G and Petrasek J (2015) Nat Rev GastroenterolHepatol 12:387-400.; herein incorporated by reference in their entireties). Therefore, high levels of these molecules in serum could represent altered homeostasis, but the specific injured tissue may be difficult to ascertain because of their overall broad tissue distribution. The mitochondrial enzyme carbamoyl phosphate synthetase-1 (CPS1) is released into the bloodstream during acute liver injury in humans and mice (Weerasinghe et al. (2014) Am J Physiol Gastrointest Liver Physiol 307:G355-364.; herein incorporated by reference in its entirety). CPS1 is the most abundant mitochondrial matrix protein with long half-life (7.7 days) in hepatocytes (Clarke S (1976) J Biol Chem. 251:950-961.; Nicoletti M, et al. (1977) Eur J Biochem. 75:583-592.; herein incorporated by reference in their entireties). It is a 160 kDa protein, composed of multi-domains catalyzing synthesis of carbamoyl phosphate from ammonia and bicarbonate, which is important to remove excessive ammonia from the portal blood in the first step in the urea cycle (de Cima S et al. (2015) Sci Rep 5:16950.; Pekkala S et al. (2010) HumMutat 31:801-808.; herein incorporated by reference in their entireties). CPS1 expression is highly enriched in parenchyma of the liver with much lower expression in the small intestine and even lower levels in other tissues. CPS1 is a potential prognostic serum marker of liver injury because of its preferential expression in the liver, its short serum half-life as compared with other liver enzymes such as alanine aminotransferase, and its abundance (Weerasinghe et al. (2014) Am J Physiol GastrointestLiver Physiol 307:G355-364.; herein incorporated by reference in its entirety). However, the role of CPS1 in blood and the significance of its short half-life have been unknown. Recent work suggests that CPS1 levels, which is barely detectable in normal lung, correlate negatively with survival of patients harboring non-small cell lung cancer. SUMMARY Provided herein are compositions methods for the treatment and/or prevention of liver injury. In particular, carbamoyl phosphate synthatase-1 (CPS-1) peptides and polypeptides (e.g., enzymatically active or inactive CPS-1 peptides and polypeptides), and methods of use thereof for the treatment and/or prevention of liver injury are provided. In some embodiments, provided herein are compositions comprising a CPS1 polypeptide having at least 70% (e.g., 70%, 75%, 80%, 85%, 90%, 95%, 99%, 100%, or ranges therebetween) sequence identity (or similarity) to all or a portion of SEQ ID NO: 1, wherein the composition is not a product of nature, and wherein the CPS1 polypeptide exhibits a cytokine like activity of wild-type of CPS1. In some embodiments, the CPS1 polypeptide comprises at least 70% (e.g., 70%, 75%, 80%, 85%, 90%, 95%, 99%, 100%, or ranges therebetween) sequence identity to one or a combination of SEQ ID NOs: 2-8 (e.g., at least 70% sequence identity with SEQ ID NOs: 2-7, 2-6, 2-5, 2-4, 2-3, 3-7, 3-6, 3-5, 3-4, 4-7, 4-6, 4-5, 5-7, 5-6, 2 and 4-7, 2 and 5-7, 2 and 6-7, 2 and 7, 2-3 and 5-7, 2-3 and 6-7, 2-3 and 7, 2-4 and 5-7, 2-4 and 6-7, 2-4 and 7, 2-5 and 7, 2-3 and 4-7, 2-3 and 5-7, 2-3 and 6-7, 2-3 and 7, and any other suitable combinations of included an excluded domains). In some embodiments, the CPS1 polypeptide lacks a portion comprising 25% or greater sequence identity to one or more of SEQ ID NOs: 2-8 (e.g., lacks SEQ ID NO: 2, 3, 4, 5, 6, or 7; lacks SEQ ID NOs: 2-3, 2-4, 2-5, 2-6, 3-4, 3-5, 3-6, 3- 7, 4-5, 4-6, 4-7, 5-6, 5-7, 6-7, 2 and 5-7, 2 and 6-7, 2 and 7, 3 and 6-7, 3 and 7, 2 and 5, 3 and 5- 7, 3 and 6-7, 3 and 5, 3 and 6, 4 and 7, 3 and 6, or any other combination of excluded domains). In some embodiments, provided herein are compositions comprising a CPS1 peptide having at least 70% (e.g., 70%, 75%, 80%, 85%, 90%, 95%, 99%, 100%, or ranges therebetween) sequence identity (or similarity) with a portion of SEQ ID NO: 1 that is 8-30 amino acid residues in length, wherein the composition is not a product of nature, and wherein the CPS1 peptide exhibits a cytokine-like activity of wild-type of CPS1.