• Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

Card Range To Study

through

image

Play button

image

Play button

image

Progress

1/209

Click to flip

Use LEFT and RIGHT arrow keys to navigate between flashcards;

Use UP and DOWN arrow keys to flip the card;

H to show hint;

A reads text to speech;

209 Cards in this Set

  • Front
  • Back

Enzymes that use FAD

Acyl-Coa dehydrogenase


Succinate dehydrogenase (complex II)


Mitochondrial glycerol-3-P dehydrogenase

Enzymes that use PLP



Glycogen phosphorylase


Amino transferases (alanine, aspartate, tyrosine)


Serine dehydratase


Cystathionine beta-synthase


Glutamate decarboxylase


Histidine decarboxylase

Enzymes that consume GTP

PEP carboxykinase

Enzymes that produce GTP

Succinyl-Coa synthetase

Enzymes that consume TPP

Pyruvate decarboxylase


Transketolase

Enzymes that consume NADPH

Aldose reductase with galactose


Ketoacyl-ACP reductase (rev)


Enoyl-ACP reductase


Overall palmitate synthesis


HMG-CoA reductase


Squalene synthase


NO synthase


Glutathione reductase


Ribonucleotide reductase


Dihydrofolate reductase


Heme oxygenase

Enzymes that produce NADPH

Glucose-6-P dehydrogenase (rev)


6-phosphogluconate dehydrogenase


Malic enzyme


Hill reaction

Enzymes that use


TPP


FAD


Lipoate

Pyruvate dehydrogenase complex


alpha-ketoglutarate dehydrogenase complex


Branched chain alpha-ketoacid dehydrogenase complex

Enzymes that use BIOTIN

Pyruvate carboxylase


Propionyl-CoA carboxylase


Acetyl-CoA carboxylase

Name the enzymes that during the degradation of glucose lead to cleavage of covalent bonds between two C-atoms.

Aldolase (hexose -> two trioses)


Pyruvate dehydrogenase complex (release CO2)


Isocitrate dehydrogenase (release CO2)


alpha-ketoglutarate dehydrogenase (release CO2)

Which enzymes do we have in the glycolysis but not gluconeogenesis?

Hexokinase


PFK1


Pyruvate kinase



Which enzymes do we have in the gluconeogenesis but not glycolysis?

Pyruvate carboxylase


Fructose-1,6-bisphosphatase


Glucose-6-phosphatase

Which enzymes are needed for glycogen metabolism?

Hexokinase


Phosphoglucomutase


UDP-glucose pyrophosphorylase


Glycogen synthase (primer)


Glycogen branching enzyme



In which reactions is citrate an allosteric activator for lipid metabolism? (enzyme)

Acetyl-Coa carboxylase


HMG-CoA reductase



In which reactions does citrate inhibit? (enzyme)

Pyruvate kinase


PFK1

Branching points in metabolic pathway:


Glucose-6-phosphate (pathways and enzymes)

Glycolysis: phosphohexose isomerase




Pentose phospate pathway: Glucose-6-phosphate dehydrogenase




Gluconeogenesis: glucose-6-phospatase




Glycogen pathway

Branching points in metabolic pathway:


Fructose

Muscle:


Hexokinase (can also phosphorylate fructose)




Liver:


No hexokinase, but GLUCOkinase, which is specific for glucose)


Instead:


Fructokinase -> fructose-1-P


Fructose-1-P aldolase -> glyceraldehyde + dhap


Triose kinase -> glyceraldehyde -> ga3P

Fructosemia

Fructose-1-P aldolase deficiency


No gluconeogenesis - hypoglycemia

Fructosuria

Fructokinase deficiency


Diarrhea

Branching points in metabolic pathway:


DHAP

Glycolysis


Gluconeogenesis


Enzymes:


Aldolase


Triose phosphate isomerase


Glycerol-3-P dehydrogenase


(All reactions are reversible)

Mitochondrial enzymes that converts glucose to fatty acids

Citrate lyase


Pyruvate dehydrogenase complex

Branching points in metabolic pathway:


Pyruvate (enzymes)



Lactate dehydrogenase -> Lactate


(Only in muscle)


Pyruvate decarboxylase -> Acetaldehyde


Pyruvate carboxylase -> Oxaloacetate


Pyruvate dehydrogenase complex -> Acetyl-Coa


Malic enzyme -> Malate (Uses NADPH)


Alanine aminotransferase (In both muscle and liver)

Branching points in metabolic pathway:


Oxaloacetate



PEP carboxylase (rev)


Malate dehydrogenase (rev)


Aspartate aminotransferase (rev)




Consumes:


PEP carboxykinase (gluconeogenesis)


Citrate synthase (TCA)



Reversible ammonia producing/consuming reactions

Glutamate dehydrogenase


Glycine cleavage enzyme

Irreversible ammonia consuming reactions:

Glutamate synthase


Carbamoyl synthase

Irreversible ammonia producing reactions:

Desaminase (adenosine)


Serine/Threonine dehydratase


Glutaminase

Why does adipose tissue have the enzyme PEP carboxykinase, even though gluconeogenesis only happens in kidney and liver?



Glyceroneogenesis!


Glycerol-3-phosphate production

Ketone calculation:


Acetoacetate (How many ATP?)

20 ATP

Ketone calculation:


Beta-hydroxybutyric (...)

22.5 ATP

In which tissues does gluconeogenesis happen?

Kidney and liver

Comparison of cori cycle and alanine cycle.


Similarities:

Glucose goes back to muscle




Pyruvate is an acceptor molecule


(Picks up NH4+ -> produces alanine OR


Picks up proteins and electrons -> produces lactate)




(Pyruvate is produced in liver from alanine OR lactate. Enters gluconeogenesis and produces glucose -> returns to muscle)

Comparison of cori cycle and alanine cycle.


Differences:

Onset:


Cori cycle: Hypoxia


Alanine cycle: Starvation




Transporting molecule


Cori cycle: Lactate (is transported to liver from muscle)


Alanine cycle: Alanine (is transported to liver from muscle)

Describe glucose-6-phosphate dehydrogenase deficiency and benefits.

RBC disorder. No pentose phosphate pathway, so no NADPH formation. Glutathione reductase doesn't work, so free radicals are not neutralized. Free radicals attack hemoglobin's globin chains -> globin precipitates as HEINZ BODIES. This alters the membrane deformability of RBCs.




BUT: It can protect against malaria - because malaria lives in RBCs (which are destroyed). Therefore there is a bigger prevalence of G6PDH deficiency in countries with malaria.

Which molecules can transport toxic ammoniac?

Glutamine (from brain), alanine (from muscle) and glutamate (other tissues)

Components (?) needed purines

CO2


Glycine


Aspartic acid


Glutamate


THF

Components (?) needed for pyrimidines

Aspartic acid


Carbamoyl phosphate

Degradation of nucleotides:


Reaction


Inhibitor


Disease treated with inhibitor

Xanthine oxidase


Inhibitor: allopurinol


Disease: Gout

Helicase (DnaB protein)

Unwinds DNA

Primase (DnaG protein)

Synthesizes RNA primers

Single-stranded DNA-binding protein (SSB)

Binds single-stranded DNA

RNA polymerase

Facilitates DnaA activity (DnaA - Recognizes ori sequence)

DNA topoisomerase II

Separates new and original strand in replication

DNA ligase

Links okazaki fragments

Dam methylase

Methylates (5')GATC sequences at ori

Which activity does DNA polymerase III have?

5'-3' Elongation activity


3'-5' Exonuclease activity

Which activity does DNA polymerase I have?

5'-3' Elongation activity


5'-3' Exonuclease activity

DNA polymerase III function

New strand elongation

DNA polymerase I function

Fills gaps

Enzymes needed for Human Mismatch repair

Dam methylase


MutH, MutL, MutS proteins


DNA helicase II


SSB


DNA polymerase III


Exonuclease I, VII, X


RecJ nuclease


DNA ligase

Function of exonuclease in DNA repair

Removes abnormal region

Enzymes needed for Base excision repair

DNA glycosylases


AP endonucleases


DNA polymerase I


DNA ligase

Function of base excision repair

Removal of damaged region and replacement by new DNA

Function of DNA glycosylase

Removes damaged base at AP-site

Type of damage for nucleotide excision repair

DNA lesions that cause large structural changes. E.g. pyrimidine dimers

Nucleotide excision repair enzymes

ABC exinuclease


DNA polymerase I


DNA ligase

Reaction impaired in Phenylketonuria

Phenylalanine hydroxylase


Phenylalanine -> Tyrosine

Reactions impaired in Maple syrup urine disease



Reactions impaired in Tyrosinemia type I

Fumarylacetoacetate


Fumarylacetoacetate -> Fumarate + acetoacetate

Reactions impaired in Tyrosinemia type II

Tyrosine aminotransferase

Reactions impaired in Tyrosinemia type III

Hydroxyphenylpyruvate dioxygenase




Hydroxyphenylpyruvate -> Homogenisate

Reactions impaired in Citrullinemia type I

Argininosuccinate synthetase




Citrulline + Aspartate -> Argininosuccinate

Reactions impaired in Homocystinuria

Cystathione beta-synthase




Cysteine + Serine -> cystathione

Reactions impaired in (Hyper)argininemia

Arginase




Arginine -> ornithine + urea

Reactions impaired in Lesch-Nyhan syndrome



____ Phosphoribosyltransferase




Adenine + PRPP -> AMP + PPi


Hypoxanthine + PRPP -> IMP + PPi


Guanine + PRPP -> GMP + PPi

Reactions impaired in Arginosuccinate lyase deficiency

Argininosuccinate lyase




Arginosuccinate -><- Arginine + Fumarate

Reactions impaired in beta-ketothiolase deficiency

Acyl-Coa acetyltransferase




Ketoacyl-CoA -> Acyl-CoA + Acetyl-CoA

Reactions impaired in Methylmalonic acidemia

Methylmalonyl-CoA mutase




Methylmalonyl-Coa -> Succinyl-CoA

Reactions impaired in propionic acidemia

Propionyl-CoA carboxylase




Propionyl-CoA -> Methylmalonyl-CoA

Reactions that leads to the formation of galactose metabolite potentially causing cataract

Aldose reductase with galactose




Galactose -> Galactitol

Name the enzymes that their defect can lead to galactosemia

Gal-1-P Uridyltransferase


Galactokinase


UDP-Gal-4 epimerase

What are the sources of propionyl-CoA in methylmalonic acidemia?

Amino acids


Odd chained fatty acids


Propionate

List the defected carboxylase enzymes in


multiple carboxylase deficiency and biotinidase deficiency

Pyruvate carboxylase


Propionyl-CoA carboxylase


Acetyl-Coa carboxylase


Methylcrotonyl-Coa carboxylase

List the possible causes of permanent congenital hypothyreosis?

Thyroid gland dysgenesis


Defects in thyroid hormone synthesis or secretion


Defects in thyroid hormone transport


Central hypothyroidism

Proteins required to initiate replication in prokaryotes

DnaA protein


DnaB protein (Helicase)


DnaC protein


HU (Histone-like protein)


Primase (DnaG protein)


SSB


RNA polymerase


DNA gyrase (DNA topoisomerase II)


Dam methylase

Proteins at prokaryotic replication fork

SSB


DnaB protein (helicase)


Primase (DnaG protein)


DNA polymerase III


DNA polymerase I


DNA ligase


DNA gyrase (DNA topoisomerase II)

Direct repair

DNA photylases


O6-methylguanine-DNA methyltransferase


AlkB protein

Type of damage for mismatch repair

Mismatches

Typoe of damage for base excision repair

Abnormal bases (uracil, hypoxanthine, xanthine), alkylated bases

Type of damage for Direct repair

DNA photylases:


Pyrimidine dimers


O6-Methylguanine-DNA methyltransferase:


O6-Methylguanine


AlkB protein:


1-Methylguanine, 3-methylcytosine

Endonuclease

Cleaves inside DNA

Exonuclease

Cleaves on either 5' or 3' end

Exinuclease

Special endonuclease. Cleaves twice - is a part of nucleotide excision repair (ABC exinuclease)

Which metabolites are needed for the AlkB function?

Succinyl-Coa


alpha-ketoglutarate

DNA and RNA polymerase: Similarities

Direction of synthesis: 5'-3'


Mechanism of elongation


Hydrolysis of pyrophosphate


Processivity

What is special for RNA polymerase?

No polyA og polyG


Don't need a primer


No nuclease activity


Template: one strand of DNA, certain genes

What is the replication fork?

The sites where DNA synthesis occurs

What is another name for DNA gyrase, and where are they found?

Topoisomerase II


Only prokaryotes

Which DNA polymerases have proofreading ability?

All of them

What kind of activity is proofreading activity?

Nuclease activity

What is a protein with no enzymatic activity?

SSB

What is a nucleotide polymerase in the replication fork that doesn't have proofreading ability/nuclease activity?

Primase - RNA polymerase

Which molecule is responsible when there is a methylation of a cytosine group, and what kind of repair is it?

AlkB protein


Direct repair

Which molecule is responsible when there is a methylation of a guanine group, and what kind of repair is it?

O6-Methylguanine-DNA methyltransferase


Point mutation

Endonuclease

Cleaves inside

Exonuclease

Cleaves either at 5' or 3' end

Exinuclease

Special endonuclease


Cleaves twice - part of nucleotide excision repair

Which metabolites are needed for Alk-B protein process?

Succinyl-CoA and alpha-ketoglutarate. The protein needs an acceptor of the methyl group. Direct repair enzyme.

What is the direction of synthesis in transcription?

5'-3'

What determines transcription start sites?

Promoter regions

What are the prokaryotic promoter regions?

-35


-10 (Pribnow box)


+1 (transcription start site)

What are the eukaryotic promoter regions?

TATA box

What do the -10 region and TATA box have in common?

AT rich regions

How many RNA polymerases are needed in prokaryotic transcription?

1

What does the holoenzyme consist of and is it in prokaryotes or eukaryotes?

alpha2betabetaprime = core enzyme


sigma subunit = subunit




prokaryotes





What is the purpose of the holoenzyme?

Aids in BINDING gene and STARTING transcription. Sigma hops off after a few nucleotides are added.

What is the transcription machinery in eukaryotic transcription?

3 RNA polymerases:


RNA Pol I: rRNA


RNA Pol II: mRNA


RNA Pol III: tRNA (+ 5S rRNA)

What are transcription factors?

Proteins that aid in transcription

Termination in prokaryotes

Rho-independent = intrinsic


-> Forms a hairpin loop (Inverted repeats)




Rho-dependent termination


-> rho protein travels along the RNA transcript until it reaches the RNA polymerase

Post-transcriptional modifications

ONLY IN EUKARYOTES!


mRNA:


1. 5'Cap: 7-methylguanosine


2. 3' Poly(A) tail = Poly Adenylate


3. Splicing

5' Cap

7-Methylguanosine


- Aids in transport from nucleus to cytoplasm


- Protects 5' end from degradation

3' Poly(A) tail enzyme

Polyadenylate polymerase


Protects 3' end from degradation

Splicing

By spliceosome - contains snRNP


- Lariat structure formed


- Introns are removed


- Exons are kept

Where does transcription and translation happen in prokaryotes?

Cytosol


At the same time

Where does transcription and translation happen in eukaryotes?

Transcription: Nucleus


Translation: Cytosol


- Different time

What does it mean that 1 mRNA codes for 1 protein, and in prokaryotes or eukaryotes?

Monocistronic


Eukaryotes

What does it mean that 1 mRNA codes for


several proteins, and in prokaryotes or eukaryotes?

Polycistronic


Prokaryotes

Which human genes have no introns?

Mitochondrial DNA


Histones

What are the differences in mRNA in


eukaryotes


mitochondria


prokaryotes

Eukaryotic: Cap, poly(A) tail


Mitochondrial: No cap, Poly(A) tail


Prokaryotic: No intron, no cap

How does histone acetylation affect gene expression?

It activates it (transcription)

How does histone deacetylation affect gene expression?

It inhibits it (transcription)

Gene expression is also regulated by ...

Epigenetic processes!



What are epigenetic processes?

GC-rich regions after promotor regions

What kind of proteins catalyzes/regulates the rate of folding?

Chaperones!

What type of chaperones are there and what are their functions?

Small chaperones -> activates folding + foldase


Lactin-like chaperones -> Quality control

What is another thing chaperones regulate?

Unfolded protein degradation

Which enzymatic activities do we have during folding?

Cleavage


Forming of secondary bonds


ATP hydrolysis (we need energy)

Where is carbohydrate modification done?

ER -> glycosylation


Golgi -> the rest

What is the difference between glycation and glycosylation?

Glycation:


Chemical process. E.g. too much glucose - affects hemoglobin - can be used diagnostically to determine blood glucose level.




Glycosylation:


Enzymatic process

What are inhibitors of HMG-CoA reductase?

Statins

Why does tumor development decrease in patients that take cholesterol medication (?) (STATINS)

RAS oncogene is also activated in the membrane - mutation - can't cleave




CHECK THIS

What is responsible for activation and attachment of amino acid to tRNA

Aminoacyl-tRNAs (synthase?)




CHECK

tRNA


Made by and process mechanisms

RNA Pol III




Process mechanisms:


3'+5' ends are cleaved


Splicing


CCA arm attachment


Modification of nucleotides

rRNA

RNA pol I


RNA pol III - 5S rRNA

What is a ribozyme?

RNA molecules with enzymatic activity

What kind of enzymatic activities does ribozymes have?

Peptidyl transferase activity

Modifications of rRNA

Methylation


Pseudouridylated




Done by snoRNA

Types of splicing of mRNA

1. Spontaneous. External guanosine


2. Spontaneous. Intron has adenosine. Lasso formation.


3. Spliceosome dependent. (U1, U2, U4, U5, U6) by snRNP.

Aminoacyl-tRNA synthase

Proofreading activity

When doesn't aminoacyl-tRNA synthase's proofreading ability work?

If the side chain has the same solubility


e.g. leucine + isoleucine

Mechanisms that ensure accuracy of translation

Proofreading: aminoacyl-tRNA synthase


Proofreading: peptidyl-transferase


2nd genetic code


Wobble

Which protein needs saline?

Glutathione peroxidase

Ligases in prokaryotes and eukaryotes. Process.

Prok: Adenylation (AMP donor is NADH+)


Euk: Adenylation (AMP donor is ATP)

Enzymes of glycogen degradation

- Glycogen phosphorylase


- Glycogen debranching enzyme


- Phosphoglucomutase


- Glucose-6-phosphatase

Regulation of glycogen phosphorylase in muscle and liver

Muscle:


Activators: epinephrine, high [Ca2+], high [AMP]




Liver:


Activators: Glucagon


Inhibitors: Insulin

How is glycogen synthase activated?

By dephosphorylation by PP1

What activates and inhibits PP1?

Activated by:


- glucose


-glc-6-p


-insulin




Inhibited by:


-glucagon


-epinephrine

How is glycogen synthase inhibited?

By phosphorylation by GSK3 (glycogen synthase kinase 3)

What is the direct covalent regulator for GS and GPh?

PP1

Why isn't PKA the direct covalent regulator for GS and GPh?

Direct for GS


Indirect for GPh

What is the last common precursor for storage lipids and membrane phospholipids?

Phosphatidic acid

Which proteins are required to produce blood glucose from glucose-6-phosphate?

G6P transporter


Glucose-6-phosphatase


Glucose transporter


Phosphate transporter


GLUT2

Which enzymatic activity does the debranching enzyme have?

It destroys the branches:




1. Transferase activity


2. Glycosidase activity

How is glycogen metabolism regulated?

Allosteric


Covalent


Hormonal


Gene expression


Glycogen targeting proteins

What are the similarities of glucokinase and hexokinase?

Both convert glucose into glucose-6-phosphate

Glucokinase vs. hexokinase:


Substrate specificity

Hk: Phosphorylates all hexoses


Gk: Only phosphorylates glucose

Glucokinase vs. hexokinase:


Sensitivity/affinity

Hk: High affinity for glucose


Gk: Low

Glucokinase vs. hexokinase:


Location

Hk: Muscle cells


Gk: Liver cells



Both glucagon and insulin induce phosphorylation of Gm, but the effect is opposite. Explain why.

Because Gm doesn't become inactive until it's been phosphorylated twice!

What is the hormonal regulation of gluconeogenesis?

Insulin -> INHIBIT




Glucagon, epinephrine, glucocorticoids -> ACTIVATE

What is the effect of EPINEPHRINE on Glycogenolysis in liver and muscle?

Both increase

What is the effect of EPINEPHRINE on Glycolysis in liver and muscle?

Liver: Decrease
Muscle: Increase

What are the non-essential amino acids and what molecule do they derive from?

Alanine <- alpha-ketoglutarate


Asparagine <- 3-phosphoglycerate


Aspartate <- oxaloacetate


Glutamate <- aspartate


Serine <- Pyruvate

Glutamate biosynthesis

Transamination of alpha-ketoglutarate


Glutamate dehydrogenase reaction


Glutamate synthase reaction

What kind of activity is special for DNA


polymerase I in prokaryotes?

In addition to 5'-3' elongation activity and 3'-5' exonuclease it has:




5'-3' EXONUCLEASE ACTIVITY!


Removal of RNA primers!

What inhibits both pro- and eukaryotic RNA polymerases?

Actinomycin D

What is the function of Actinomycin D?

Inhibits both pro- and eukaryotic RNA polymerases

What is the substance that inhibits prokaryotic RNA pol beta subunit?

Rifampicin

What is the function of Rifampicin?

Inhibits prokaryotic RNA polymerase beta subunit

Which substance inhibits pol II and pol III in eukaryotes?

alpha-amantin

What is the function of alpha-amantin

Inhibits eukaryotic Pol II and pol III

Regulation of transcription

Strength of promoter


+1: G or A


Activator/repressor molecules


sigma factors


Attenuation (premature termination of transcription)


Antitermination

What is attenuation?

Premature termination of transcription

RNA Pol I


Location


Product


alpha-amantin sensitivity

Nucleolus




rRNA,


18S, 28S, 5.8S rRNA




Resistant



RNA Pol II


Location


Product


alpha-amantin sensitivity

Extranucleolar




pre-mRNA, miRNA, snRNA




Highly sensitive

RNA Pol III


Location


Product


Alpha-amantin sensitivity

Nucleus, chromatin




tRNA, 5S rRNA, snRNA




Moderately sensitive

Function of mRNA

Encode the amino acid sequence of one or more polypeptides specified by a gene/a set of genes

Function of tRNA

Reads the information encoded in the mRNA and transfer an amino acid to the growing polypeptide chain in protein synthesis

Function of rRNA

Forms the core structure of the ribosome

Function of miRNA

MicroRNA


Post-transcriptional regulators

Function of siRNA

Small interfering RNA


Binds to mRNA and silence it

Function of saRNA

Small activating RNA


Induces long lasting gene activation

Function of snRNA

Small nuclear RNA




Processes pre-mRNA in the nucleus. Part of the spliceosome

Function of snoRNA

Small nucleolar RNA




Help process and assemble RNAs

piRNA

Piwi-interacting RNA




Transcriptional gene silencing of retrotransposons in germ line cells

rasiRNA

Repeat associated small interfering RNA




Silences transposons and retrotransposons


Establishes and maintains heterochromatin structure

qiRNA

Induced by DNA damage. When there is a DNA damage, it inhibits protein translation

tmRNA

Transfer messenger RNA




Rescues ribosomes. Facilitates degradation of non-normal mRNA

Vitamin B1

Thiamine


TPP

Vitamin B2

Riboflavin.


Flavin mononucleotide = FAD

FMN

In complex I

Vitamin B3

Niacin.


NAD and NADPH

B5

Pantothenic acid


CoA

B6

Pyridoxyl


PLP

B7

Vitamin H = Folic acid




Glycine cleavage


Nucleotide biosynthesis

B12

Methylmalonyl-CoA mutase


Methionine beta-synthase

Vitamin C

Hydroxylation


Collagen (if deficient -> scurvy)


Liver (detoxification)


Synthesis of carnitine

Vitamin D

Not a vitamin (we can produce it)


Cholesterol in liver -> skin -> liver -> kidney -> 1,25dihydroxycalciferol = calcitriol

Which receptors does hormones have?

Nuclear receptors

Where is the attachment of Receptor and hormone in Vitamin D?

In the nucleus

What is the coreceptor of Vitamin D?

RXR Receptor



Which ligands have RXR receptor?

Retinoic acid


Thyroid hormones


Vitamin D

Vitamin K

Filakinan


Blood coagulation

Vitamin E

Binds free radicals


Only lipid-soluble antioxidant


Sperm maturation (If deficient -> sterility)

Vitamin A

Vision.

Insulin excretion channels

Ion channels in beta cells: GLUT2


Na+ gated K+ channels (ATP-dependent)


Voltage dependent K+ channels

Endocrine hormones

Insulin


Glucagon

Paracrine

Eicosanoid

Autocrine

Interleukins -> regulate cytokines

How to write poly(a) tail in an exam?

Poly adenylate tail