Amino acids do not suppress proteolysis in premature neonates

B B Poindexter1, C A Karn, C A Leitch

  • 1Section of Neonatal-Perinatal Medicine, Department of Pediatrics, Indiana University School of Medicine, 699 West Dr. RR208, Indianapolis, IN 46202, USA. bpoindex@iupui.edu

Insights

Premature infants do not reduce protein breakdown with increased amino acids, unlike full-term infants. However, they can increase essential amino acid metabolism, crucial for meeting nutritional needs.

Area of Science:

  • Biochemistry
  • Neonatal Physiology
  • Nutritional Science

Background:

  • Premature neonates have unique metabolic needs and challenges.
  • Understanding amino acid metabolism is vital for optimizing nutrition in preterm infants.
  • Proteolysis and amino acid catabolism regulation may differ in premature infants.

Purpose of the Study:

  • To investigate if increased amino acid availability reduces proteolysis in premature neonates.
  • To assess the premature infant's capacity for essential amino acid catabolism (leucine oxidation, phenylalanine hydroxylation).
  • To determine if amino acids stimulate glucose production in premature neonates.

Main Methods:

  • Measured leucine and phenylalanine kinetics in premature infants (32 wk gestation) during the first week of life.
  • Administered graded infusions of intravenous amino acids (1.2 and 2.4 g.kg(-1).day(-1)).
  • Assessed endogenous rates of appearance (proteolysis), leucine oxidation, phenylalanine hydroxylation, and glucose production.

Main Results:

  • Amino acid infusion did not suppress proteolysis in premature infants, unlike in full-term neonates.
  • Leucine oxidation and phenylalanine hydroxylation increased stepwise with amino acid infusion.
  • Endogenous glucose production remained unchanged despite amino acid administration.

Conclusions:

  • Premature neonates exhibit a different response to amino acid availability regarding proteolysis compared to full-term infants.
  • Premature infants possess the capacity to increase essential amino acid catabolism, potentially vital for tyrosine synthesis.
  • Amino acids do not stimulate glucose production in premature neonates during the first week of life.

Related Concept Videos

Protein Digestion01:02

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
Amino acids03:42

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
Proteins: Dietary Sources and Requirements01:28

Proteins: Dietary Sources and Requirements

Consuming animal-based products offers high-quality proteins that contain optimal levels and combinations of essential amino acids, crucial for tissue repair and growth. Foods like eggs, milk, fish, and most meats are a source of complete proteins. Legumes and cereals are abundant in proteins; however, they typically lack a full range of essential amino acids. As a result, they are considered incomplete protein sources. Some plant sources like soybeans, quinoa, and amaranth do contain complete...
Overview of Protein Metabolism01:21

Overview of Protein Metabolism

Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
Amino Acid Catabolism01:18

Amino Acid Catabolism

Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which provide...